\r\n\tThis book will provide information about fouling mitigation in general and the ecofriendly methods of fouling mitigation. Chapters from this book will inform the readers about fouling models and predictive maintenance of the equipment prone to fouling. Adaptive means for prolonged continuous operation will also be addressed. This book will guide the readers in selection of fouling mitigation approaches for different applications. A brief discussion on economic impact of fouling in different industries will also be part of this book.
",isbn:null,printIsbn:"979-953-307-X-X",pdfIsbn:null,doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!1,hash:"f31d1d99cc6caac249973b404ae9091a",bookSignature:"Dr. Salim Newaz Kazi",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/9022.jpg",keywords:"Scales and Deposits, Water Chemistry, Types of Fouling, Mechanism of Fouling, Fouling in Chemical Industries, Fouling in Dairy Industries, Membrane and Filtration, Membrane Fouling, Characterize Scales, Dissolution of Deposits, Conventional Fouling Mitigation, Ecofriendly Ways of Mitigation",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:null,numberOfDimensionsCitations:null,numberOfTotalCitations:null,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"May 16th 2019",dateEndSecondStepPublish:"February 14th 2020",dateEndThirdStepPublish:"April 14th 2020",dateEndFourthStepPublish:"July 3rd 2020",dateEndFifthStepPublish:"September 1st 2020",remainingDaysToSecondStep:"a year",secondStepPassed:!0,currentStepOfPublishingProcess:5,editedByType:null,kuFlag:!1,biosketch:null,coeditorOneBiosketch:null,coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"93483",title:"Dr.",name:"Salim Newaz",middleName:null,surname:"Kazi",slug:"salim-newaz-kazi",fullName:"Salim Newaz Kazi",profilePictureURL:"https://mts.intechopen.com/storage/users/93483/images/system/93483.jfif",biography:"Kazi Md Salim Newaz, Ph.D., is a Professor in the Department of Mechanical Engineering, Faculty of Engineering, University of Malaya. \r\nHe has 11 years of service experience as an academic and 18 years of engineering service experience in petrochemical industries, construction of different chemical plants and engineering consultant in the international arena. He has the academic background with B. Sc. in Engineering (Mechanical), Master of Science in Mechanical Engineering, Master of Engineering (Mechanical) and Ph. D. in Heat transfer and Fouling Mitigation. \r\nHe has been working at University of Malaya since 2009. He has introduced sophisticated research approaches on heat transfer, particle characterization, fiber and paper, heat exchanger fouling and corrosion mitigation, separation flow, nanofluid synthesis and applications, renewable energy, etc. He has completed supervision of 21Ph.D. theses, 7 patents, published more than 165 technical papers, 10 technical book chapters and edited 4 engineering books.",institutionString:"University of Malaya",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"4",totalChapterViews:"0",totalEditedBooks:"4",institution:{name:"University of Malaya",institutionURL:null,country:{name:"Malaysia"}}}],coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"6",title:"Biochemistry, Genetics and Molecular Biology",slug:"biochemistry-genetics-and-molecular-biology"}],chapters:null,productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},personalPublishingAssistant:{id:"280415",firstName:"Josip",lastName:"Knapic",middleName:null,title:"Mr.",imageUrl:"https://mts.intechopen.com/storage/users/280415/images/8050_n.jpg",email:"josip@intechopen.com",biography:"As an Author Service Manager my responsibilities include monitoring and facilitating all publishing activities for authors and editors. From chapter submission and review, to approval and revision, copy-editing and design, until final publication, I work closely with authors and editors to ensure a simple and easy publishing process. I maintain constant and effective communication with authors, editors and reviewers, which allows for a level of personal support that enables contributors to fully commit and concentrate on the chapters they are writing, editing, or reviewing. I assist authors in the preparation of their full chapter submissions and track important deadlines and ensure they are met. I help to coordinate internal processes such as linguistic review, and monitor the technical aspects of the process. As an ASM I am also involved in the acquisition of editors. Whether that be identifying an exceptional author and proposing an editorship collaboration, or contacting researchers who would like the opportunity to work with IntechOpen, I establish and help manage author and editor acquisition and contact."}},relatedBooks:[{type:"book",id:"2230",title:"An Overview of Heat Transfer Phenomena",subtitle:null,isOpenForSubmission:!1,hash:"7bb8831521deb0cadc8f29532d083b50",slug:"an-overview-of-heat-transfer-phenomena",bookSignature:"Salim N. Kazi",coverURL:"https://cdn.intechopen.com/books/images_new/2230.jpg",editedByType:"Edited by",editors:[{id:"93483",title:"Dr.",name:"Salim Newaz",surname:"Kazi",slug:"salim-newaz-kazi",fullName:"Salim Newaz Kazi"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"3091",title:"Heat Transfer Phenomena and Applications",subtitle:null,isOpenForSubmission:!1,hash:"8536c61b1e94dd17840626e6546dea99",slug:"heat-transfer-phenomena-and-applications",bookSignature:"Salim N. 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Therefore, it is part of cell biology but mainly deals with an interphase between analytical methods such as X-ray crystallography producing models at atomic or molecular resolution, and direct nanoscale imaging with high resolution microscopes such as scanning probe microscopes, electron microscopes and super-resolution microscopes. Several cell structures are involved in nanoscale processes (Figure 1).
\nThe main flow of genetic information represented as the so-called central dogma of molecular biology in situ, illustrates the major secretory pathway in the cell (Figure 2).
\nDuring this pathway, nanoscale particles represent substrates of different moments. During transcription, nuclear particles are involved in transcription and processing of RNA, both, pre-mRNA and pre-rRNA. pre-mRNA is transcribed and processed in the nucleoplasm while pre-rRNA is transcribed and processed within the nucleolus, the major known ribonucleoproteins structure where ribosome biogenesis and other functions of eukaryotic cell take place. Once in the cytoplasm, translation takes place in the ribosome, also a major ribonucleoprotein particle of 10-15 nm in diameter. When the synthesized protein contains a signal peptide, it is translocated into the rough endoplasmic reticulum, helped by the signal recognition particle or SRP, another major and conserved ribonucleoprotein. The transport to Golgi apparatus by the intermediated zone and the TGN producing the three derivatives from the Golgi apparatus are mediated by vesicles [see 1].
\nCell nanobiology proposes to study cell structures using in situ high resolution microscopical approaches as electron and atomic force microscopy that could complement molecular and biochemical data to better understand a physiological role at the nanoscale.
Semenogelin
Semenogelin is the most abundant protein in the semen of mammals. It is a glycosylated protein that is responsible for properties such as density. As an example, the semenogelin of the tamarin Saguinus oedipus is used to show how the signals in the nucleic acids and proteins determine the intracellular pathways associated to that expression. Its expression includes intranuclear events as transcription by RNA polymerase II from a split gene consisting of 3 exones and 2 intrones, processing of the transcript as 5’ end methylation, 3’ polyadenylation and splicing. All of them are associated to nuclear particles. Once in the cytoplasm, the mature transcript or mRNA associates to a ribosome that in turns translates the transcript. If the resulting protein contains a signal peptide, the signal recognition particle or SRP -a very well conserved RNA+protein complex- binds to it and associates to the rough endoplasmic reticulum, giving rise to the translocation process that introduces that protein to the lumen. Once there, N-glycosylation takes place at several asparagine residues following the basic rule of adjacent aminoacids showing a basic rule as Asn-X(except proline)-Ser or Asn. In S. oedipus semenogelin, there are 14 N-glycosylation sites. The protein then continues flowing through the Golgi apparatus or complex and at the TGN a secretory vesicle forms containing the protein that finally is secreted by the epithelial cell of seminal vesicle. The analysis of the gene sequences, as well as the transcription, processing, translation and post-translational products can predict the cell structures involved in the process [see 1].
\nA general overview of the cell structure and function. The diagram illustrates the in situ flow of genetic information of a secretory protein encoded in the genome within the cell nucleus. A gene is copied into a pre-mRNA that is processed to mRNA within the nucleus. mRNA in the cytoplasm may contain a signal sequence that allows entrance to rough endoplasmic reticulum and further to Golgi complex. The protein inside a vesicle is secreted out of the cell.
There are many cell structures or products made by cells that could be analyzed under the present approach. Some of them are indicted in Figure 1, but there are others as extracellular matriz components, cytoskeleton elements, etc.; virus are also nanometric structures associated always to cell organelles. Here we will give an overview of some of the cell components, as examples.
\nNuclear particles
In eukaryote cells, transcription and processing mainly takes place within the cell nucleus, associated to nuclear particles that are well known since a method for ribonucleoprotein (RNP) structures was described in 1969 [2]. These particles are few nanometers in diameter or lengh. To date, several nuclear RNPs have been described including involved in mRNA metabolism: perichromatin fibers, perichromatin granules, interchromatin granules in mammals. In insects, Balbiani ring granules are well known structures [3]. In 1992 Lacandonia granules were described for some plants [4]. In addition, other nuclear bodies around 300-400 nm in diameter have been described involved in gene expression. As for rRNA transcription and processing, the nucleolus is a nuclear organelle containing pre-ribosomes in the granular component that are about 10-20 nm in diameter.
\nRough endoplasmic reticulum particles
The ribosome
Ribosomes are the universal ribonucleoprotein particles that translate the genetic code into proteins. The shape and dimensions of the ribosome were first visualized by electron microscopy [6-8]. Ribosomes have diameters of about 25 nanometers in size and are roughly two-thirds RNA and one-third protein. All ribosomes have two subunits, one about twice the mass of the other. The ribosome basic structure and functions are well-known. There are 70S ribosomes common to prokaryotes and 80S ribosomes common to eukaryotes. The bacterial ribosome is composed of 3 RNA molecules and more than 50 proteins. In humans, the small ribosome unit has 1 large RNA molecule and about 32 proteins; the large subunit has 3 RNA molecules, and about 46 proteins. Each subunit has thousands of nucleotides and amino acids, with hundreds of thousands of atoms. The small subunit (0.85 MDa) initiates mRNA engagement, decodes the message, governs mRNA and tRNA translocation, and controls fidelity of codon–anticodon interactions and the large subunit catalyzes peptide bond formation.
\nIn 1980, the first three-dimensional crystals of the ribosomal 50S subunit from the thermophile bacterium Geobacillus stearothermophilus were reported [9]. Since then, ribosome crystallography advanced rapidly. To date crystal structures have been determined for the large ribosomal subunit from the archaeon Haloarcula marismortui at 2.4 Å [10] and the 30S ribosomal subunit from Thermus thermophilus [11]. The structure of the entire 70S ribosome in complex with tRNA ligands (at 5.5Å resolution) emerged shortly after the structures of the initial subunits [12].
\nLacandonia granules are nanoscale (32 nm in diameter) and abundant particles (arrows) in the nucleoplasm of the plant Lacandonia schismatica. Transmission electron microscopy image of a cell in the teguments of the flower. Cc, compact chromatin.
Snapshots of ribosome intermediates provided by cryo-EM and x-ray crystallography, associated translation factors, and transfer RNA (tRNA) have allowed dynamic aspects of protein translation to be reconstructed. For example, recent cryo-EM reconstructions of translating ribosomes allowed direct visualization of the nascent polypeptide chain inside the ribosomal tunnel at subnanometer resolution [13-15]. The dimension of the ribosomal tunnel in bacterial, archaeal, and eukaryotic cytoplasmic ribosomes is conserved in evolution [16 -18]. The ribosomal tunnel in the large ribosomal subunit is ~80 Å long, 10–20 Å wide, and predominantly composed of core rRNA [19]. The tunnel is clearly not just a passive conduit for the nascent chain, but rather a compartment in a dynamic molecular dialogue with the nascent chain. This interplay might not only affect the structure and function of the ribosome and associated factors, but also the conformation and folding of the nascent chain [20]. As the nascent polypeptide chain is being synthesized, it passes through a tunnel within the large subunit and emerges at the solvent side, where protein folding occurs.
\nPeptide bond formation on the bacterial ribosome and perhaps on the ribosomes from all organisms is catalyzed by ribosomal RNA as well as ribosomal protein and also by the 2’-OH group of the peptidyl-tRNA substrate in the P site. The high resolution crystal structures of two ribosomal complexes from T. thermophilus [21] revealed that ribosomal proteins L27 and L16 of the 50S subunit stabilize the CCA-ends of both tRNAs in the peptidyl-transfer reaction, suggesting that peptide chains from both these proteins take part in the catalytic mechanism of peptide bond formation.
\nNucleolus of a PtK2 cell. Within the cell nucleus (N), the nucleolus displays three different components named fibrillar center (fc), dense fibrillar component (dfc) and granular components (g). In the inset, a high magnification of the nucleolus shows granular particles or pre-ribosomes in the granular component (g). In the cytoplasm (c), ribosomes are also visible (arrow).
Representation of a prokaryotic (a) and a eukaryotic ribosome (a). Each one is an RNP is constituted by two subunits, each containing rRNA and proteins. b) a model to show the nanoscale morphology of a mammalian cytoplasmic ribosome (small [S] and large [L] subunits).
Ribosomes mediate protein synthesis by decoding the information carried by messenger RNAs (mRNAs) and catalyzing peptide bond formation between amino acids. When bacterial ribosomes stall on incomplete messages, the trans-translation quality control mechanism is activated by the transfer-messenger RNA bound to small protein B (tmRNA–SmpB ribonucleoprotein complex). Trans-translation liberates the stalled ribosomes and triggers degradation of the incomplete proteins. The cryo-electron microscopy structures of tmRNA–SmpB accommodated or translocated into stalled ribosomes demonstrate how tmRNA–SmpB crosses the ribosome and how as the problematic mRNA is ejected, the tmRNA resume codon is placed onto the ribosomal decoding site by new contacts between SmpB and the nucleotides upstream of the tag-encoding sequence [22]. Recently, the crystal structure of a tmRNA fragment, SmpB and elongation factor Tu bound to the ribosome shows how SmpB plays the role of both the anticodon loop of tRNA and portions of mRNA to facilitate decoding in the absence of an mRNA codon in the A site of the ribosome [23].
\nThe structure of the ribosome at high resolution reveals the molecular details of the antibiotic-binding sites, explain how drugs exercise their inhibitory effects. Also, the crystal structures help us to speculate about how existing drugs might be improved, or novel drugs created, to circumvent resistance [24]. Recently, ribosome engineering has emerged as a new tool to promote new crystal forms and improve our knowledge of protein synthesis. To explore the crystallization of functional complexes of ribosomes with GTPase, a mutant 70S ribosomes were used to crystallize and solve the structure of the ribosome with EF-G, GDP and fusidic acid in a previously unobserved crystal form [25].
\nIn contrast to their bacterial counterparts, eukaryotic ribosomes are much larger and more complex, containing additional rRNA in the form of so-called expansion segments (ES) as well as many additional r-proteins and r-protein extensions [26]. The first structural models for the eukaryotic (yeast) ribosome were built using 15-A° cryo–electron microscopy (cryo-EM) maps fitted with structures of the bacterial SSU [11] and archaeal LSU [10], thus identifying the location of a total of 46 eukaryotic r-proteins with bacterial and/or archaeal homologs as well as many ES [27].
\nRibosome biogenesis is regulated by the conserved protein kinase TOR (target of rapamycin), a member of the ATM-family protein. TOR up-regulates transcription of rRNA and mRNA for ribosomal proteins in both yeast and mammals [28-30]. Recent results indicate that in yeast, conserved kinases of the LAMMER/Cdc-like and GSK-3 families function downstream of TOR complex 1 to repress ribosome and tRNA synthesis in response to nutrient limitation and other types of cellular stress [31].
\nThe signal recognition particle (SRP)
The Signal Recognition Particle (SRP) is an evolutionarily conserved rod-shaped 11S ribonucleoprotein particle, 5–6 nm wide and 23–24 nm long [32]. It comprises an essential component of the cellular machinery responsible for the co-translational targeting of proteins to their proper membrane destinations [33].
\nAlthough SRP is essential and present in all kingdoms of life maintaining its general function, structurally it shows high diversity. Vertebrates SRP consists of a single ~ 300-bp RNA (SRP RNA or 7S RNA) and six polypeptides designated SRP9, SRP14, SRP19, SRP54, SRP68 and SRP72. It can be divided into two major functional domains: the Alu domain (comprising the proteins SRP9 and -14) and the S domain (SRP19, -54, -68, and -72). The S domain functions in signal sequence recognition and SR interaction, whereas the Alu domain is required for translational arrest on signal sequence recognition [34]. In Archaea and Eucarya, the conserved ribonucleoproteic core is composed of two proteins, the accessory protein SRP19, the essential GTPase SRP54, and an evolutionarily conserved and essential SRP RNA [35]. SRP54, comprises an N-terminal domain (N, a four-helix bundle), a central GTPase domain [G, a ras-like GTPase fold, with an additional unique α-β- α insertion box domain (IBD)], and a methionine-rich C-terminal domain [36-37]. The N and G domains are structurally and functionally coupled; together, they build the NG domain that is connected to the M domain through a flexible linker [38]. The M domain anchors SRP54 to SRP RNA and carries out the principal function of signal sequence recognition [39-41]. The NG domain interacts with the SR in a GTP-dependent manner [43].
\nSRP is partially assembled in the nucleus and partially in the nucleolus. In agreement with that, nuclear localization for SRP proteins SRP9/14, SRP68, SRP72 and SRP19 has been determined [44]. After the transport into the nucleus the subunits bind SRP RNA and form a pre-SRP which is exported to the cytoplasm where the final protein, Srp54p, is incorporated [45-47]. Although this outline of the SRP assembly pathway has been determined, factors that facilitate this and/or function in quality control of the RNA are poorly understood [48]. SRP assembly starts during 7S RNA transcription by RNA polymerase III in the nucleolus, by binding of the SRP 9/14 heterodimer and formation of Alu-domain. Prior to transportation to the nucleus SRP9 and SRP14 form the heterodimer in the cytoplasm, a prerequisite for the binding to 7S RNA [49].
\nThe signal recognition particle displays three main activities in the process of cotranslational targeting: (I) binding to signal sequences emerging from the translating ribosome, (II) pausing of peptide elongation, and (III) promotion of protein translocation through docking to the membrane-bound SRP receptor (FtsY in prokaryotes) and transfer of the ribosome nascent chain complex (RNC) to the protein-conducting channel [50]. Despite the diversity of signal sequences, SRP productively recognizes and selectively binds them, and this binding event serves as the critical sorting step in protein localization within the cell. The structural details that confer on SRP this distinctive ability are poorly understood. SRP signal sequences are characterized by a core of 8–12 hydrophobic amino acids that preferentially form an α-helix, but are otherwise highly divergent in length, shape, and amino acid composition [51-52]. This and the unusual abundance of methionine in the SRP54 M-domain led to the ‘methionine bristle’ hypothesis, in which the flexible side chains of methionine provide a hydrophobic environment with sufficient plasticity to accommodate diverse signal sequences [53].
\nThe signal recognition particle. During protein synthesis of the secretory pathway, the signal peptide binds to SRP, an RNP particle containing a small RNA and 6 different proteins (b, [modified from 60]). A model for SRP at nanoscale is shown in (c).
In the SRP pathway, SRP binds to the ribosome synthesizing the polypeptide, and subsequently also binds an SRP receptor, located next to the machinery that transfers proteins across the membrane and out of the cell. This process begins when a nascent polypeptide carrying a signal sequence emerges from the translating ribosome and is recognized by the SRP. The ribosome-nascent chain complex is delivered to the target membrane via the interaction of SRP with the SRP receptor. There, the cargo is transferred to the Sec61p (or secYEG in archaea and bacteria) translocon, which translocates the growing polypeptide across the membrane or integrates it into the membrane bilayer. SRP and SR then dissociate from one another to enter subsequent rounds of targeting.
\nDuring the last years, several structures have been solved by crystallography and cryo-electron microscopy that represent distinct functional states of the SRP cycle. On this basis, the first structure-based models can be suggested that explain important aspects of protein targeting, such as the SRP–ribosome [54], SRP-SRP receptor [55] and SRP–SR interactions. The snapshots obtained by single-particle EM reconstructions enable us to follow the path of a nascent protein from the peptidyl-transferase center, through the ribosomal tunnel, to and across the translocon in the membrane. With new developments in image processing techniques it is possible to sort a biological homogenous sample into different conformational states and to reach subnanometer resolution such that folding of the nascent chain into secondary structure elements can be directly visualized [56].
\nMolecular biology, biochemistry, and cryo-electron microscopy, have been combined to study the ribosome-protein complexes involved in protein assembly, folding and targeting. These approaches led to obtain structural snapshots of entire pathways by which proteins are synthesized and targeted to their final positions. The link between SRP and its receptor is usually transient and chemically unstable, for this reason, engineered SRP receptor bind more stably to SRP, then introduced to ribosomes and observed the resulting complexes using cryo-electron microscopy (cryo-EM). Cryo-EM can be performed in roughly physiological conditions, providing a picture that closely resembles what happens in living cells. This picture can then be combined with higher-resolution crystallography data and biochemical studies [57-58].
\nPeroxisomes
The oxidative stress (EO) is a disorder where reactive oxygen species (ROS) are produced. These compounds, that include free radicals and peroxides, play important roles in cell redox signaling. However, disturbances in the balance between the ROS production and the biological system can be particularly destructive. For example, the P450 oxide reductase activity produces H2O2 as a metabolite. This enormous family of enzymes is present in the mitochondrial and smooth endoplasmic reticulum (SER) membranes and catalyzes several reactions in the pathway of the biogenesis of steroid hormones [59] and in the detoxification process or in the first stage of drugs or xenobiotics hydrolysis, converting them in the SER, in water-soluble compounds for its excretion in the urine [60-62].
\nPeroxisomes are single membrane organelles present in practically every eukaryotic cell. Matrix proteins of peroxisomes synthesized in free polyribosomes in the cytoplasm and imported by a specific signal, are encoded in genes present in the cell nucleus genome. Peroxisomal membrane-bound PEX proteins, also encoded in the nuclear genome, are synthetized by ribosomes associated to rough endoplasmic reticulum since they display signal peptide. Therefore the peroxisome as an organelle derives from the rough endoplasmic reticulum. These organelles participate in ROS generation, as H2O2, but also in cell rescue from oxidative stress by catalase activity. In several biological models for pathological processes involving oxygen metabolites, the role of peroxisomes in prevention of oxidative stress is strongly suggested by de co-localization of catalase and H2O2, and the induction of peroxisomes proliferation [63].
\nMitochondrion and chloroplast particles
ATP synthase: A rotary molecular motor
To support life, cells must be continuously supplied with external energy in form of light or nutrients and must be equipped with chemical devices to convert these external energy sources into adenosine triphosphate (ATP). ATP is the universal energy currency of living cells and as such is used to drive numerous energy-consuming reactions, e.g., syntheses of biomolecules, muscle contraction, mechanical motility and transport through membranes, regulatory networks, and nerve conduction. When performing work, ATP is usually converted to ADP and phosphate. It must therefore continuously be regenerated from these compounds to continue the cell energy cycle. The importance of this cycle can be best illustrated by the demand of 50 Kg of ATP in a human body on average [64].
\nProkaryotes use their plasma membrane to produce ATP. Eukaryotes use instead the specialized membrane inside energy-converting organelles, mitochondria and chloroplasts, to produce most of their ATP. The mitochondria are present in the cells of practically all eukaryotic organisms (including fungi, animals, plants, algae and protozoa), and chloroplasts occur only in plants and algae. The most striking morphological feature of both organelles, revealed by electron microscopy, is the large amount of internal membrane they contain. This internal membrane provides the framework for an elaborate set of electron-transport processes, mediated by the enzymes of the Respiratory Chain that are essential to the process of Oxidative Phosphorylation which generate most of the cell’s ATP.
\nIn eukaryotes, oxidative phosphorylation occurs in mitochondria and photophosphorylation in chloroplasts. In the mitochondria, the energy to drive the synthesis of ATP derive from the oxidative steps in the degradation of carbohydrates, fats and amino acids; whereas the chloroplasts capture the energy of sunlight and harness it to make ATP [60].
\nThe Chemiosmotic Model of Peter Mitchell
Our current understanding of ATP synthesis in mitochondria and chloroplasts is based on the chemiosmotic model proposed by Peter Mitchell in 1961 [60], which has been accepted as one of the great unifying principles of twentieth century. According with this model, the electrochemical energy inherent in the difference in proton concentration and the separation of charge across the inner mitochondrial membrane (the proton motive force) drives the synthesis of ATP as protons flow passively back into the matrix through a proton pore associated with the ATP synthase (Fig. 7).
\nUnder aerobic conditions, the major ATP synthesis pathway is oxidative phosphorylation of which the terminal reaction is catalyzed by F\n \n O\n \n F\n \n 1\n\n -ATP synthase. This enzyme is found widely in the biological world, including in thylakoid membranes, the mitochondrial inner membrane and the plasma membrane of bacteria, and is the central enzyme of energy metabolism in most organisms [65].
\nIn the mitochondrion (a), ATP synthase (arrow in a; b) is part of the respiratory chain.
Like many transporters the F\n \n O\n \n F\n \n 1\n -ATP synthase (or F-type ATPase) has been fascinating subject for study of a complex membrane-associated process. This enzyme catalyzes ATP synthesis from adenosine diphosphate (ADP) and inorganic phosphate (Pi), by using the electrochemical potential of protons (or sodium ions in some bacteria) across the membrane, i.e. it converts the electrochemical potential into its chemical form. ATP synthase also functions in the reverse direction (ATPase) when the electrochemical potential becomes insufficient: it catalyzes proton pumping to form an electrochemical potential to hydrolyze ATP into ADP and Pi. Proton translocation and ATP synthesis (or hydrolysis) are coupled by a unique mechanism, subunit rotation. Electrochemically energy contained in the proton gradient is converted into mechanical energy in form of subunit rotation, and back into chemical energy as ATP (Nakamoto RK, et al, 2008).
\nMitochondrial ATP synthase is an F-type ATPase similar in structure and mechanism to the ATP synthases of chloroplasts and bacteria. This large complex of the inner mitochondrial membrane, also called Complex V, catalyzes the formation of ATP from ADP and Pi, accompanied by the flow of protons from P (positive) side to N (negative) side of the membrane [66].
\n\n F\n O\n F\n \n 1\n -ATP Synthase Structure and Function
ATP synthase is a supercomplex enzyme with a molecular weight of 500 kDal and consists of two rotary motors. One is F\n \n 1\n subcomplex (~380 kDal), which is the water-soluble part of ATP synthase. F\n \n 1\n was identified and purified by Efraim Racker and his colleagues in the early 1960s. When isolated from the membrane portion, it acts as an ATP-driven motor: it rotates its inner subunit to hydrolyze ATP and is therefore term F\n \n 1\n ATPase. The other rotary motor of ATP synthase is the membrane-embedded Fo subcomplex (~120 kDal) through which the protons flow.
\nIn the simplest form of the enzyme, in bacteria like Escherichia coli, F\n \n 1\n is composed of five different subunits, in a stoichiometry of α3β3γδε, and F\n \n O\n consists of three distinct subunits in a stoichiometry of ab\n \n 2\n \n c\n \n 10-15\n . A newer more mechanically-based division differentiates between the “rotor” (in E. coli,γεcn) and the “stator” (α\n \n 3\n \n β\n \n 3\n \n δab\n \n 2\n ). The α3α3 ring of the stator contains the three catalytic nucleotide sites, on the β subunits at the interphase to the adjacent α subunit. The a subunit contains the static portion of the proton traslocator machinery. α3β3 and a are held together by the “stator stalk” (or “peripheral stalk”), consisting of b\n \n 2\n γ [65].
\nThe crystallographic determination of the F\n \n 1\n\n structure by John Walker and colleagues [67] revealed structural details very helpful in explaining the catalytic mechanism of the enzyme. The three α- and β- subunits that constitute the hexameric stator ring are alternately arranged like the sections of an orange. The rotor shaft is the γ-subunit, which is accommodated in the central cavity of the α3β3-ring. The ε-subunit binds onto the protruding part of the γ-subunit and provides a connection between the rotor parts of F\n \n 1\n and F\n \n O\n . The δ-subunit acts as a connector between F\n \n 1\n and F\n \n O\n that connects the stator parts.
\nCatalytic reaction centers for ATP hydrolysis/synthesis reside at the three of the α-β interfaces, whereas the non-catalytic ATP-binding sites reside on the other α/β interfaces. While the catalytic site is formed mainly with amino acid residues from γ-subunit, the non- catalytic sites are primarily within the α-subunit. Upon ATP hydrolysis on the catalytic sites, F\n \n 1\n rotates the γ-subunit in the anticlockwise direction viewed from the F\n \n O\n side [68].
\nAs mentioned before, F\n \n O\n subcomplex (o denoting oligomycin sensitive) consists of ab\n \n 2\n \n c\n \n 10-15\n subunits. The number of c subunits varies among the species and form a ring complex by aligning in a circle. It is widely thought that the c-ring and the a subunit form a proton pathway. With the downhill proton flow through the proton channel, the c-ring rotates against the ab\n \n 2\n subunits in the opposite direction of the γ-subunit of the F\n \n 1\n motor [69]. Thus, in the F\n \n O\n \n F\n \n 1\n complex, F\n \n O\n and F\n \n 1\n push each other in the opposite direction. Under physiological condition where the electrochemical potential of the protons is large enough to surpass the free energy of ATP hydrolysis, F\n \n O\n forcibly rotates the γ-subunit in the clockwise direction and then F\n \n 1\n catalyzes the reverse reaction, i.e. ATP synthesis which is the principle function of ATP synthase. In contrast, when the electrochemical potential is small or decreases, F\n \n 1\n forces F\n \n O\n to rotate the c-ring in the reverse direction to pump protons against the electrochemical potential.
\nThe c subunit of the F\n \n O\n complex is a small (Mr 8,000), very hydrophobic polypeptide, consisting almost entirely of two membrane-spanning α-helices, that are connected by a small loop extending from the matrix side of the membrane. The crystal structure of the yeast F\n \n O\n \n F\n \n 1\n , solved in 1999, shows the arrangement of the subunits. The yeast complex has 10 c subunits, each with two transmembrane helices roughly perpendicular to the plane of the membrane and arranged in two concentric circles. The inner circle is made up of the amino-terminal helices of each c subunit; the outer circle, about 55 Å in diameter, is made up of the carboxyl-terminal helices. The ε andγ subunits of F\n \n 1\n form a leg-and-foot that projects from the bottom (membrane) side of F\n \n 1\n and stands firmly on the ring of c subunits. The a subunit is a very hydrophobic protein that in most models is composed of five transmembrane helices. Ion translocation takes place through subunit a and its interface with subunit c. The b subunits are anchored within the membrane by an N-terminal α-helix and extend as a peripheral stalk all the way to the head of the F\n \n 1\n\n domain. According to cross-linking studies, the b subunits contact de C-terminal part of the c subunit and the loop between helices 4 and 5 of the a subunit at the periplasmic surface. The δ-subunit forms a strong complex with the α-subunit. In mitochondria, the peripheral stalk consists of more subunits named OSCP (Oligomycin Sensitive Conferring Protein), b, δ and F6 [64].
\nStructure of F\n \n 1\n and binding-change mechanism for ATP Synthesis.
The classic working model for F1 is the “binding-change mechanism” proposed by Paul Boyer [70]. The early stage of this model postulated an alternating transition between two chemical states, assuming two catalytic sites residing on F\n \n 1\n . It was later revised to propose the cyclic transition of the catalytic sites based on the biochemical and electron microscopic experiments that revealed that F\n \n 1\n has the three catalytic sites [71-73]. One important feature of this model is that the affinity for nucleotide in each catalytic site is different from each other at any given time, and the status of the three β-subunits cooperatively change in one direction accompanying γ rotation. This hypothesis is strongly supported by X-ray crystallographic studies performed by Walker’s group [67] that first resolved crystal structure of F\n \n 1\n , which revealed many essential structural features of F\n \n 1\n at atomic resolution. Importantly, the catalytic β-subunits differ from each other in conformation and catalytic state: one binds to an ATP analogue, adenosine 5’-(β,γ-imino)-triphosphate (AMP-PNP), the second binds to ADP and the third site is empty. Therefore, these sites are termed βTP, βDP and βEmpty, respectively. While βTP and βDP have a close conformation wrapping bound nucleotides on the catalytic sites, βEmpty has an open conformation swinging the C-terminal domain away from the binding site to open the cleft of the catalytic site. These features are consistent with the binding-change mechanism. Another important feature found in the crystal is that while the N-terminal domains of the α- and β-subunits form a symmetrical smooth cavity as the bearing for γ rotation at the bottom of the α3β3-ring, the C-terminal domains of the β-subunit show distinct asymmetric interactions with the γ-subunit. Therefore, the most feasible inference is that the open-to-closed transition of the β-subunits upon ATP binding pushes γ, and the sequential conformational change among β- subunits leads the unidirectional γ rotation.
\nOne strong prediction of the binding-change model of Boyer is that the γ subunit should rotate in one direction when F\n \n O\n \n F\n \n 1\n\n is synthesizing ATP and in the opposite direction when the enzyme is hydrolyzing ATP. This prediction was confirmed in elegant experiments in the laboratories of Masasuke Yoshida and Kazuhiko Kinosita Jr. [74]. The rotation of γ in a single F\n \n 1\n molecule was observed microscopically by attaching a long, thin, fluorescent actin polymer to γ and watching it move relative to α\n \n 3\n \n β\n \n 3\n immobilized on a microscope slide, as ATP was hydrolyzed [see 75]. Lately the unidirectional γ rotation was visualized in simultaneous imaging of the conformational change of the β-subunit and the γ rotation.
\nNew approaches for studying biological macromolecules.
The Atomic Force Microscope (AFM) is a powerful tool for imaging individual biological molecules attached to a substrate and place in aqueous solution. This technology allows visualization of biomolecules under physiological conditions. However, it is limited by the speed at which it can successively record highly resolved images. Recent advances have improved the time resolution of the technique from minutes to tens of milliseconds, allowing single biomolecules to be watch in action in real time. Toshio Ando and his coworkers at Kanazawa University have been leading innovators in this so-called High-Speed Atomic Force Microscope (HS-AFM) technology [76]. This technology allows direct visualization of dynamic structural changes and dynamic processes of functioning biological molecules in physiological solutions, at high spatial-temporal resolution. Dynamic molecular events appear in detail in an AFM movie, facilitating our understanding of how biological molecules operate to function.
\nIn this regard, the Ando group showed a striking example of molecular motor action in their AFM movies of the isolated subcomplex of the rotary motor protein F\n \n 1\n -ATPase. Previous single-molecule experiments on parts of this enzyme had measured rotation, but they could only be done if at least one subunit of the rotor was attached. The AFM, however, could visualize the conformational change that the β subunits of the stator undergo when they bind ATP. By imaging at 12.5 frames/s, the authors followed the time dependence of these conformational changes, leading to the surprising conclusion that, contrary to what was widely assumed before, the catalysis on the enzyme maintains its sequential rotary order even in absence of the rotor subunits.
\n“To directly observe biological molecules at work was a holy grail in biology. Efforts over the last two decades at last materialized this long-quested dream. In high-resolution AFM movies, we can see how molecules are dynamically behaving, changing their structure and interacting with other molecules, and hence we can quickly understand in stunning detail how molecules operate to function. This new approach will spread over the world and widely applied to a vast array of biological issues, leading to a number of new discoveries. The extension of high-speed AFM to a tool for imaging live cells, which allows direct in situ observation of dynamic processes of molecules and organelles, remains an exciting challenge but will be made in the near future because it is a right and fruitful goal” [77].
\nLipid rafts
Cell membranes are dynamic assemblies of a variety of lipids and proteins. They form a protective layer around the cell and mediate the communication with the outside world. The original fluid mosaic model [78] of membranes suggested a homogenous distribution of proteins and lipids across the two-dimensional surface, but more recent evidence suggests that membranes themselves are not uniform and that microdomains of lipids in a more ordered state exist within the generally disorder lipid milieu of the membrane. These clusters of ordered lipids are now referred to as lipid rafts [79] (Pike LJ 2009).
\nLipid rafts (LRs), consist of cell membrane domains rich in cholesterol, sphingolipids and lipid-anchored proteins in the exoplasmic leaflet of the lipid bilayer. Because of their ability to sequester specific lipids and proteins and exclude others, rafts have been postulated to perform critical roles in a number of normal cellular processes, such as signal transduction [80], membrane fusion, organization of the cytoskeleton [81-83], lipid sorting, and protein trafficking/recycling, as well as pathological events [84].
\nLRs are too small to be resolved by standard light microscopy - they range from 10 to about 200 nm - with a variable life span in the order of milliseconds (msec). Detergent resistant membranes, containing clusters of many rafts, can be isolated by extraction with Triton X-100 or other detergents on ice. However, this method involves breaking up the membrane and has limitations in terms of defining the size, properties, and dynamics of intact microdomains [85-88].Thus, a variety of sophisticated techniques have recently been used to analyze in detail open questions concerning rafts in cell and model membranes including biochemical, biophysical, quantitative fluorescence microscopy, atomic force microscopy and computational methodologies [89-90].
\nComponents of a lipid raft. (1) non raft membrane, (2) lipid raft, (3) lipid raft associated transmembrane protein, (4) GPI-anchored protein, (5) glycosylation modifications (glycoproteins and glycolipids).
The raft affinity of a given protein can be modulated by intra- or extracellular stimuli. Saturated fatty acids are preferentially enriched in the side chains of the membrane phospholipids, which allows closer packing and thus increased rigidity, more order and less fluidity of the LRs compared to the surrounding membrane [91-92]. Proteins with raft affinity include glycosylphosphatidylinositol (GPI)-anchored proteins [93-94], doubly acylated proteins, such as Src-family kinases or the α-subunits of heterotrimeric G proteins8, cholesterol-linked and palmitoylated proteins such as Hedgehog9, and transmembrane proteins, particularly palmitoylated ones [92-95].
\nDifferent subtypes of lipid rafts can be distinguished according to their protein and lipid composition. Caveolae are types of rafts that are rich in proteins of the caveolin family (caveolin-1, -2 and -3) which present a distinct signaling platform [96]. The caveolae are enriched in cholesterol, glycosphingolipids, and sphingomyelin. They are the site of several important protein–protein interactions, for example, the neurotrophin receptors, TrkA and p75(NTR), whose respective interactions with caveolin regulates neurotrophin signaling in the brain. Caveolins also regulate G-proteins, MAPK, PI3K, and Src tyrosine kinases.
\nThe most important role of rafts at the cell surface may be their function in signal transduction. Lipid rafts have been implicated as the sites for a great number of signaling pathways.They form concentrating platforms for individual receptors, activated by ligand binding [86]. If receptor activation takes place in a lipid raft, the signaling complex is protected from non-raft enzymes such as membrane phosphatases that otherwise could affect the signaling process. In general, raft binding recruits proteins to a new micro-environment, where the phosphorylation state can be modified by local kinases and phosphatases, resulting in downstream signalling. Individual signaling molecules within the raft are activated only for a short period of time.
\nImmobilization of signaling molecules by cytoskeletal actin filaments and scaffold proteins may facilitate more efficient signal transmission from rafts [97]. Current evidence supports a role for lipid rafts in the initiation and regulation of The B-cell receptor signaling and antigen trafficking [98-100]. The importance of lipid raft signalling in the pathogenesis of a variety of conditions, such as Alzheimer’s, Parkinson’s, cardiovascular and prion diseases, systemic lupus erythematosus and HIV, has been elucidated over recent years[ 101] and makes these specific membrane domains an interesting target for pharmacological approaches in the cure and prevention of these diseases [102]. Rafts serve as a portal of entry for various pathogens and toxins, such as human immunodeficiency virus 1 (HIV-1). In the case of HIV-1, raft microdomains mediate the lateral assemblies and the conformational changes required for fusion of HIV-1 with the host cell [103]. Lipid rafts are also preferential sites of formation for pathological forms of the prion protein (PrPSc) and of the β-amyloid peptide associated with Alzheimer’s disease {104].
\nPlasma membranes typically contain higher concentrations of cholesterol and sphingomyelin than do internal membranous organelles [105-106]. Thus, along the secretion pathway, there are very low concentrations of cholesterol and sphingolipids in the endoplasmic reticulum, but the concentrations of these lipids increase from the cis-Golgi to the trans-Golgi and then to the plasma membrane [107-108]. On the contrary, recent evidence suggests that mitochondria do not contain lipid rafts, and lipid rafts do not contain mitochondrial proteins [109].
\nLipid raft domains play a key role in the regulation of exocytosis [110]. The association of SNAREs protein complexes with lipid rafts acts to concentrate these proteins at defined sites of the plasma membrane that are of functional importance for exocytosis [111-114].
\nThe nucleolus
The cell nucleus contains different compartments that are characterized by the absence of delineating membranes that isolate it from the rest of the nucleoplasm [5]. Due to the high concentration of RNA and proteins that form it, the nucleolus is the most conspicuous nuclear body in cycling cells observed by light and electron microscopy. Nucleoli are formed around nucleolar organizer regions (NORs), which are composed of cluster of ribosomal genes (rDNA) repeat units [115-121]. The number of NOR-bearing chromosomes varies depending on the species, can be found 1 in haploid yeast cells to 10 in human somatic cells (short arms of chromosomes 13, 14, 15, 21 and 22). Nucleolus is the organelle of rDNA transcription by RNA polymerase I, whose activity generates a long ribosomal precursor (pre-rRNA), this molecule is the target of an extensive process that includes removing or cutting the spacers and 2\'-O-methylation of riboses and coversions of uridine residues into pseudouridines. The net result of these reactions is the release of mature species of ribosomal RNA (rRNA) 18S, 5.8S and 28S. These particles are assembled with approximately 82 ribosomal proteins and rRNA 5S (synthesized by RNA polymerase III) to form the 40S and 60S subunits; both of these subunits are then exported separately to the cytoplasm and are further modified to form mature ribosomal subunits. Currently, it is widely accepted that nucleolar transcription and early pre-rRNA processing take place in the fibrillar portion of nucleolus while the later steps of processing and ribosome subnits assembly occurs mainly in the granular zone. The architecture of the nucleolus reflects the vectorial maturation of the pre-ribosomes. The nucleolar structure is organized by three canonical subdomains that are morphologically and biochemically different. The fibrillar centers (FC), dense fibrillar component (DFC) and granular component (GC). The FCs are structures with a low electron density, often circular shape of ~0.1 to 1µm in diameter. The FCs are enriched with rDNA, RNA polymerase I, topoisomerase I and upstream binding factor (UBF). DFCs are a compact fibrillar region containing a high concentration of ribonucleoprotein molecules that confer a high electrodensity. This component entirely or partially surrounds the FCs. DFCs contains important proteins such as fibrillarin and nucleolin as well as small nucleolar RNAs, pre-rRNA and some transcription factors. FCs and DFCs are embedded in the GC, composed mainly of granules of 15 to 20nm in diameter with a loosely organized distribution. In the GC are located B23/nucleophosmin, Nop 52, r-proteins, auxiliary assembly factors, and the 40S and 60S subunits that the GC is itself composed of at least two distintc molecular domains. Considering the species, cell type and physiological state of the cell, there is considerable diversity in the prevalence and arrangement of the three nucleolar components.
\nOn the other hand, the current eukaryotic nucleolus is involved in the ribosomal biogenesis but has been described as a multifunctional entity. Extra ribosomal functions include biogenesis and/or maturation of other ribonucleoprotein machines, including the signal recognition particle, the spliceosomal small nuclear RNPs and telomerase, processing or export of some mRNAs and tRNA, cell cycle and cell proliferation control, stress response and apoptosis [116]. The plurifunctional nucleolus hypothesis is reinforced by the description of nucleolar proteome of several eukaryotes. A proteomic analysis has identified more than 200 nucleolar proteins in Arabidopsis and almost 700 proteins in the nucleolus of HeLa cells. A comparison of nucleolar proteome from humans and budding yeast showed that ~90% of human nucleolar proteins have yeast homologues. Interestingly, only 30% of the human nucleolar proteome is intended for ribosomal biogenesis [120, 122].
\nFundamental to approach the cell at the nanoscale in cell nanobiology are the classical and also remarkably new types of microscopy. Three different epochs characterize microscopy: 1) Light microscopy, developed since ca. 1500, where glass lenses and light as source of illumination are used to get resolution of up to 0.2 µm. Different types such as bright field, phase contrast, differential interference contrast (Nomarsky), dark field, polarization, fluorescence, confocal, and super-resolution, are variants of this type of microscopy. 2) Electron microscopy, developed since early 1930s, where electromagnetic lenses and electrons as source of illumination are used to get resolution of up to nm or A°. Transmission and scanning electron microscopy –including the environmental and high resolution modes- are the two forms of this microscopy. 3) Scanning probe microscopy, developed in the early 1980s, where no lenses or illuminations are used, but instead the microscope consists of a fine tip interacting with the samples to potentially obtaining atomic resolution. Scanning tunneling microscopy and atomic force microscopy are the major variants of this type of modern microscopy. Because atomic force microscopy may produce images at high resolution even under liquid, we have been using such microscopy for imaging the cell components. To test this approach, we used several cell types and generated images at low magnification (Figure 9a). Nuclear particles i.e. Lacandonia granules were already visualized using this approach (Figure 9b).
\na) Atomic force microscopy image of a cell from the tegument of the plant Lacandonia schismatica. Cell wall (CW), vacuole (V), cytoplasm (Cy), Within the nucleus (N), compact chromatin (cc), nucleolus (nu), nucleolar organizer (small arrow) and nuclear pore (large arrow). b) Atomic force microscopy of Lacandonia granules within the nucleus of a tegument cell of the plant Lacandonia schismatica. Three dimensional displaying shows compact chromatin (cc) and associated particles (arrow).
Further research in our laboratory will focusing in visualizing the nanoscale cell structures involved in fundamental processes as ribosome biogenesis, at a high resolution in situ under liquid conditions to perform quantitative analysis.
\nA view of the cell emphasizing vertical resolution obtained by atomic force microscopy may represent a way to understand cell structure and function at the nanoscale, an interphase between molecular biology and cell biology.
\nDGAPA-UNAM PAPIIT IN-227810, PAPIME PE211412, CONACyT 180835.
\nRogelio Fragoso-Soriano and Tomás Nepomuceno-Mejía are postdoctoral fellows from ICyTDF and DGAPA-UNAM at Faculty of Sciences-UNAM, respectively. Georgina Alvarez-Fernandez is on-a leave-of-absence from the Department of Biochemistry, Faculty of Medicine, UNAM. Luis and Teresa Jiménez Segura for SRP and ATP synthase figures.
\nThe rapid growth of global population as well as industrialization has led to a concomitant increase in environmental pollution. This has very negative effects on natural elements that are vital for life on earth such as air and water. It becomes very crucial therefore to find sustainable ways to mitigate pollution in order to provide a clean and safe environment for humans. Photocatalysis has attracted worldwide interest due to its potential to use solar energy not only to solve environmental problems but also provide a renewable and sustainable energy source. An efficient photocatalyst converts solar energy into chemical energy which can be used for environmental and energy applications such as water treatment, air purification, self-cleaning surfaces, hydrogen production by water cleavage and CO2 conversion to hydrocarbon fuels.
\nResearch in the development of efficient photocatalytic materials has seen significant progress in the last 2 decades with a large number of research papers published every year. Improvements in the performance of photocatalytic materials have been largely correlated with advances in nanotechnology. Of many materials that have been studied for photocatalysis, titanium dioxide (TiO2; titania) has been extensively researched because it possesses may merits such as high photocatalytic activity, excellent physical and chemical stability, low cost, non-corrosive, nontoxicity and high availability [1, 2, 3, 4]. The photocatalytic activity of titania depends on its phase. It exists in three crystalline phases; the anatase, rutile and brookite. The anatase phase is metastable and has a higher photocatalytic activity, while the rutile phase is more chemically stable but less active. Some titania with a mixture of both anatase and rutile phases exhibit higher activities compared to pure anatase and rutile phases [5, 6, 7]. When titania is irradiated with light of sufficient energy, electrons from the valence band are promoted to the conduction band, leaving an electron deficiency or hole, h+, in the valence band and an excess of negative charge in the conduction band. The free electrons in the conduction band are good reducing agents while the resultant holes in the valence band are strong oxidizing agents and can both participate in redox reactions.
\nTitania however suffers from a number of drawbacks that limit its practical applications in photocatalysis. Firstly, the photogenerated electrons and holes coexist in the titania particle and the probability of their recombination is high. This leads to low rates of the desired chemical transformations with respect to the absorbed light energy [8, 9]. The relatively large band gap energy (~ 3.2 eV) requires ultraviolet light for photoactivation, resulting in a very low efficiency in utilizing solar light. UV light accounts for only about 5% of the solar spectrum compared to visible light (45%) [1, 10]. In addition to these, because titania is non-porous and has a polar surface, it exhibits low absorption ability for non-polar organic pollutants [10, 11, 12, 13]. There is also the challenge to recover nano-sized titania particles from treated water in regards to both economic and safety concern [14]. The TiO2 nanoparticles also suffer from aggregation and agglomeration which affect the photoactivity as well as light absorption [15, 16, 17, 18]. Several strategies have been employed in the open literature to overcome these drawbacks. These strategies aim at extending the wavelength of photoactivation of TiO2 into the visible region of the spectrum thereby increasing the utilization of solar energy; preventing the electron/hole pair recombination and thus allowing more charge carriers to successfully diffuse to the surface; increasing the absorption affinity of TiO2 towards organic pollutants as well as preventing the aggregation and agglomeration of the nano-titania particles while easing their recovery from treated water. Several reviews have been published in recent years on the development of strategies to eliminate the limitations of titania photocatalysis [1, 19, 20, 21, 22, 23, 24, 25]. Most of these however focus on pollutant removal from wastewater, water splitting for hydrogen production, CO2 conversion and reaction mechanisms [1, 21, 25, 26, 27, 28, 29, 30, 31]. In this chapter, we review some of the latest publications mainly covering the last 5 years, on strategies that have been researched to overcome the limitations of TiO2 for general photocatalytic applications and the level of success that these strategies have been able to achieve. Based on the current level of research in this field, we also present some perspectives on the future of modified TiO2 photocatalysis.
\nA large number of research works have been published on TiO2 modification to enhance its photocatalytic properties. These modifications have been done in many different ways which include metal and non-metal doping, dye sensitization, surface modification, fabrication of composites with other materials and immobilization and stabilization on support structures. The properties of modified TiO2 are always intrinsically different from the pure TiO2 with regards to light absorption, charge separation, adsorption of organic pollutants, stabilization of the TiO2 particles and ease of separation of TiO2 particles.
\nMetal doping has been extensively used to advance efforts at developing modified TiO2 photocatalysts to operate efficiently under visible light. The photoactivity of metal-doped TiO2 photocatalysts depends to a large extent on the nature of the dopant ion and its nature, its level, the method used in the doping, the type of TiO2 used as well as the reaction for which the catalyst is used and the reaction conditions [32]. The mechanism of the lowering of the band gap energy of TiO2 with metal doping is shown in Figure 1. It is believed that doping TiO2 with metals results in an overlap of the Ti 3d orbitals with the d levels of the metals causing a shift in the absorption spectrum to longer wavelengths which in turn favours the use of visible light to photoactivate the TiO2.
\nBand-gap lowering mechanism of metal-doped TiO2.
Doping of TiO2 nanoparticles with Li, Na, Mg, Fe and Co by high energy ball milling with the metal nitrates was found to widen the TiO2 visible light response range. In the Na-doped sample, Ti existed as both Ti4+ and Ti3+ and the conversion between Ti4+ and Ti3+ was found to prevent the recombination of electrons and (e−) and holes (h+). The metal ion doping promoted crystal phase transformations that generated electrons (e−) and holes (h+) [33]. Mesoporous TiO2 prepared by sol gel technique and doped with different levels of Pt (1–5 wt% nominal loading) resulted in a high surface area TiO2 with an enhanced catalytic performance in photocatalytic water splitting for the Pt-doped samples. The 2.5 wt%Pt-TiO2 had showed the optimum catalytic performance and a reduction in the TiO2 band gap energy from 3.00 to 2.34 eV with an enhanced electron storage capacity, leading to a minimization of the electron-hole recombination rate [34]. Noble metal nanoparticles such as Ag [35], Pt [34], Pd [36], Rh [37] and Au [38] have also been used to modify TiO2 for photocatalysis and have been reported to efficiently hinder electron-hole recombination due to the resulting Schottky barrier at the metal-TiO2 interface. The noble metal nanoparticles act as a mediator in storing and transporting photogenerated electrons from the surface of TiO2 to an acceptor. The photocatalytic activity increases as the charge carriers recombination rate is decreased.
\nIn a recent review by Low et al. [21] the deposition of Au onto TiO2 surface is reported to result in electron transfer from photo-excited Au particles (> 420 nm) to the conduction band of TiO2, which showed a decrease in their absorption band (∼550 nm) and the band was recovered by the addition of electron donors such as Fe2+ and alcohols. Zhang et al. [39] reported that the visible light activity of coupled Au/TiO2 can be ascribed to the electric field enhancement near the metal nanoparticles. Moreover, numerous researchers coupled Au and Ag nanoparticles onto TiO2 surface to use their properties of localized surface plasmonic resonance (LSPR) in photocatalysis [40]. Wang et al. [41] and Hu et al. [42] reported an improved photocatalytic performance due to the Pt nanoparticle which increased the electron transfer rate to the oxidant. It was observed that photocatalytic sacrificial hydrogen generation was influenced by several parameters such as platinum loading (wt%) on TiO2, solution pH, and light (UV, visible and solar) intensities [43]. Moreover, complete discoloration and dye mineralization were achieved using Pt/TiO2 as catalyst; the results were attributed to the higher Pt content of the photocatalyst prepared with the highest deposition time. For Pt-TiO2 catalysts the best discoloration and dye mineralization were obtained over the catalyst prepared by photochemical deposition method and using 120 min of deposition time in the synthesis. These results may be due to the higher Pt content of the photocatalyst prepared with the highest deposition time.
\nHaung et al. [44] prepared Pt/TiO2 nanoparticles from TiO2 prepared at various hydrolysis pH values and found that the phase of TiO2 obtained depended largely on the hydrolysis pH. The anatase/rutile intersection of a Pt/TiO2 sample had a lower recombination rate compared to the anatase phase of Pt/TiO2 due to the longer recombination pathway. Though, the Pt/TiO2 anatase phase showed better degradation efficiency than the Pt/TiO2 anatase/rutile intersection. The decrease in the anatase composition of TiO2, and the decrease in the composition of TiO2 resulted in the degradation rate decrease, suggesting that anatase composition in the Pt/TiO2 system played a crucial role of increasing the photocatalytic degradation of Acid Red 1 dye.
\nLiu et al. [45] prepared the palladium doped TiO2 (Pd-TiO2) photocatalyst using chemical reduction method and tested it the photocatalytic degradation of organic pollutant. It was found that the TiO2 grain size was reduced while the specific surface area increased and the absorption of ultraviolet light also enhanced after using chemical reduction method, however, all these changes had no effect on degradation of organic pollutant. But the degradation was significantly improved due to the deposition of Pd nanoparticles; the Pd/TiO2 organic pollutant degradation was 7.3 times higher compared to TiO2 (P25).
\nRepouse et al. [46] prepared a series of noble metal promoted TiO2 (P25) by wet impregnation and found that the dispersion of the small metal crystallites on TiO2 did not affect the optical band gap of TiO2. The Pt-promoted catalyst exhibited the highest photocatalytic efficiency in the degradation of bisphenol A under solar irradiation. They also found the presence of humic acid to considerably improve the reaction rate of Rh/TiO2 but had a clearly adverse effect with P25 TiO2 photocatalyst. Fluorescence data revealed that humic acid is capable of photosensitizing the Rh/TiO2 catalyst.
\nIndium-doped TiO2 have recently been used for photocatalytic reduction of CO2 [47]. Indium doping resulted in an increase in surface area because of suppression of TiO2 particle growth during the TiO2 synthesis. The light absorption ability of the In-TiO2 was enhanced due to the introduction of the impurity level below the conduction band level of the TiO2. The photocatalytic CO2 reduction activity of the In-TiO2 was about 8 time that of pure TiO2 as a consequence of the high surface area and extended light absorption range.
\nThe doping of TiO2 with transition metals such as Cr [48], Co [48], Fe [48, 49, 50], Ni [48, 51], Mn [48, 52], V [53], Cu [54], Ni [51] and Zn [55], has been studied by different research groups. Numerous studies reported that doping of TiO2 with transition metals improve the photocatalytic activity, attributable to a change in the electronic structure resulting in the absorption region being shifted from UV to visible light. The shift results from charge-transfer transition between the d electrons of the transition metals and the conduct or valence band of TiO2 nanoparticles. Inturi et al. [48] compared the doping of TiO2 nanoparticles with Cr, Fe, V, Mn, Mo, Ce, Co, Cu, Ni, Y and Zr and it was found that Cr, Fe and V showed improved conversions in the visible region while, the incorporation of the other transition metals (Mn, Mo, Ce, Co, Cu, Ni, Y and Zr) exhibited an inhibition effect on the photocatalytic activity. The Cr-doped TiO2 demonstrated a superior catalytic performance and the rate constant was found to be approximately 8–19 times higher than the rest of the metal doped catalysts. It was reported that the reduction peaks in Cr-doped TiO2 shifted to much lower temperatures, due to the increase in the reduction potential of titania and chromium. Therefore, the higher photocatalytic efficiency of Cr/TiO2 in the visible light can be attributed to strong interaction (formation of Cr-O-Ti bonds). Fe-doped TiO2 nanoparticles were used in the visible light degradation of para-nitrophenol and it was found that the Fe-dopant concentration was crucially important in determining the activity of the catalyst. The maximum degradation rate of para-nitrophenol observed was 92% in 5 h when the Fe(3+) molar concentration was 0.05 mol%, without addition of any oxidizing reagents. The excellent photocatalytic activity was as a result of an increase in the threshold wavelength response as well as maximum separation of photogenerated charge carriers [49]. On the other hand, Fe-doped TiO2 evaluated for solar photocatalytic activity for the degradation of humic acid showed a retardation effect for the doped catalysts compared to the bare TiO2 specimens, which could be attributed to surface complexation reactions rather than the reactions taking place in aqueous medium. The faster removal rates attained by using bare TiO2 could be regarded as substrate specific rather than being related to the inefficient visible light activated catalytic performance [50]. Ola et al. [56] reported that the properties of V doped TiO2 were tuned towards visible light because of the substitution of the Ti4+ by V4+ or V5+ ions since the V4+ is centred at 770 nm while the absorption band of V5+ is lower than 570 nm. Moradi et al. [57] obtained high photocatalytic activity of Fe doped TiO2 and studied the effects of Fe3+ doping content on the band gap and size of the nanoparticles. It was found that the increase in the doping content decreased the band gap energy and particle size from 3.3 eV and 13 nm for bare TiO2 to 2.9 eV and 5 nm for Fe10-TiO2, respectively.
\nThe rare earth metals doped TiO2 catalyst also have good electron trapping properties which can result in a stronger absorption edge shift towards longer wavelength, obtaining narrow band gap. Bethanabotla et al. [58] carried out a comprehensive study on the rare earth doping into a TiO2 and found that the rare earth dopants improved the aqueous-phase photodegradation of phenol at low loadings under simulated solar irradiation, with improvements varying by catalyst composition. Differences in defect chemistry on key kinetic steps were given as the explanation for the enhanced performance of the rare earth doped samples compared to pure titania. Reszczyńska et al. [59] prepared a series of Y3+, Pr3+, Er3+ and Eu3+ modified TiO2 nanoparticles photocatalysts and results demonstrate that the incorporation of RE3+ ions into TiO2 nanoparticles resulted in blue shift of absorption edges of TiO2 nanoparticles and could be ascribed to movement of conduction band edge above the first excited state of RE3+. Moreover, incorporated RE3+ ions at the first excited state interact with the electrons of the conduction band of TiO2, resulting in a higher energy transfer from the TiO2 to RE3+ ions. But observed blue shift could be also attributed to decrease in crystallite size of RE3+–TiO2 in comparison to TiO2. The Y3+, Pr3+, Er3+ and Eu3+ modified TiO2 nanoparticles exhibited higher activity under visible light irradiation compared to pure P25 TiO2 and can be excited under visible light in the range from 420 to 450 nm. In a similar work on rare earths (Er, Yb, Ho, Tb, Gd and Pr) titania nanotubes (RE-NTs), [60] the RE3+ species were found to be located at the crystal boundaries rather than inside the TiO2 unit cell and an observed excitation into the TiO2 absorption band with resulting RE3+ emission confirmed energy migration between the TiO2 matrix and RE3+. The presence of the rare earth component was found to reduce recombination of the electrons and holes successfully by catching them and also by promoting their rapid development along the surface of TiO2 nanoparticles. Lanthanide ions doping did not impact the energy gap of TiO2 nanoparticles, however this enhanced the light absorption of catalyst. The surface range of TiO2 nanoparticles generally increases by La3+ particle doping by diminishing the crystallite size and accordingly, the doped TiO2 nanoparticle displayed higher adsorption capacity. Based on theoretical calculations, it was proposed that during the electrochemical process, new Ho-f states and surface vacancies were formed and may reduce the photon excitation energy from the valence to the conduction band under visible light irradiation. The photocatalytic activity under visible light irradiation was attributed not to ·OH but to other forms of reactive oxygen species (O2·−, HO2, H2O2).
\nTiO2 nanoparticles have been comprehensively doped at the O sites with non-metals such as C [61], B [62], I [63], F [64], S [65], and N [66]. Non-metal dopants are reported to be more appropriate for the extension of the photocatalytic activity of TiO2 into visible region compared to metal dopant [67, 68]. This can be ascribed to the impurity states which are near the valence band edge, however, they do not act as charge carriers, and their role as recombination centres might be minimized [53]. As shown in Figure 2, the mixing of the p states of the doped non-metal with the O2p states shifts the valence band edge upward and narrows the band-gap energy of the doped TiO2 photocatalyst. The nitrogen and carbon doped TiO2 nanoparticles has been reported to exhibit greater photocatalytic activity under visible light irradiation compared to other non-metal dopants.
\nBand-gap energy narrowing mechanism for non-metal-doped TiO2.
N-doped TiO2 (N-TiO2) appears to be the most efficient and extensively investigated photocatalyst for non-metal doping. Zeng et al. [69] reported the preparation of a highly active modified N-TiO2 nanoparticle via a novel modular calcination method. The excellent photocatalytic performance of the photocatalyst was ascribed to excellent crystallinity, strong light harvesting and fast separation of photogenerated carriers. Moreover, the enhancement of charge separation was attributed to the formation of paramagnetic [O-Ti4+-N2−-Ti4+-VO] cluster. The surface oxygen vacancy induced by vacuum treatment trapped electron and promoted to generate super oxygen anion radical which was a necessary active species in photocatalytic process. Phongamwong et al. [70] investigated the photocatalytic activity of CO2 reduction under visible light over modified N-TiO2 photocatalyst and they have found that the band gap of N-TiO2 photocatalyst slightly decreases with increasing N content. In addition, the sub-band energies related to the impurity energy level were observed in the N-TiO2 photocatalyst because of the interstitial N species and the sub-band gap energies were found to have decreased from 2.18 eV with 10 wt% N-TiO2 photocatalyst. In contrast, the replacement of O by N is difficult because of the radius of N (17.1 nm) being higher compared to O (14 nm) and the electroneutrality can be maintained by oxygen vacancies, that are provided by replacement of three oxygen vacancies by two nitrogen atom [71]. N-TiO2 photocatalyst reduces the oxygen energy vacancies from 4.2 to 0.6 eV, suggesting that N favors the formation of oxygen vacancies [72].
\nIn contrast, O atoms (14 nm) could be substituted easily by F atoms (13.3 nm) because of their similar ionic radius [73]. Yu et al. [64] reported that the F-doped TiO2 (F-TiO2) is able to absorb visible light due to the high-density states that were evaluated to be below the maxima valence band, although there was no shift in the band edge of TiO2. Samsudin et al. found a synergistic effect between fluorine and hydrogen in hydrogenated F-doped TiO2 which enabled light absorption in UV, visible and infrared light illumination with enhanced electrons and holes separation. Surface vacancies and Ti3+ centres of the hydrogenated F-doped catalyst coupled with enhanced surface hydrophilicity facilitated the production of surface-bound and free hydroxyl radicals. Species present on the surface of the catalyst triggered the formation of new Ti3+ occupied states under the conduction band of the hydrogenated F-doped TiO2, thus narrowing the band gap energy [73]. Enhanced photocatalytic performance of N-doped TiO2 over pure TiO2 has also been ascribed to efficient separation of electron-hole pairs as well as an increased creation of surface radicals such as hydroxyl The band gap can also be narrowed by doping TiO2 with S, since replacement of S into TiO2 can be performed easily due to larger radius of S atoms (18 nm) compared to O atoms (14 nm). S incorporation in TiO2 has been reported to change the lattice spacing of the TiO2 with a reduction in the band gap width from 3.2 to 1.7 eV allowing for higher photocatalytic activity [74]. N, S and C co-doped TiO2 samples photocatalytic reduction of Cr(IV) showed that the co-doping and calcination played an important role in the microstructure and photocatalytic activity of the catalysts. The co-doped samples calcined at 500°C showed the highest activities ascribed to the synergistic effect in enhancing crystallization of anatase and (N, S and C) co-doping. The carbon doped TiO2 (C-TiO2) is reported to be more active than N-TiO2, therefore, C-TiO2 has received special attention [75]. Noorimotlagh et al. [76] investigated the photocatalytic removal of nonylphenol (NP) compound using visible light active C-TiO2 with anatase/rutile. It was found that the doping of C into TiO2 lattice may enhance the visible light utilization and affect the structural properties of the as-synthesized photocatalysts. Moreover, it was reported that after C doping and changing the calcination temperature, the band gap was narrowed from 3.17 to 2.72 eV and from 2.72 to 2.66 eV, respectively. Ji et al. [61] reported the preparation of C-TiO2 with a diameter of around 200 nm and the tube wall was composed of anatase TiO2, amorphous carbon, crystalline carbon and carbon element doping into the lattice of TiO2. The C-TiO2 nanotubes exhibited much better performance in photocatalytic activity than bare TiO2 under UV and visible light. The obtained results were ascribed to the C doping, which narrowed the band gap energy of TiO2, extended the visible light adsorption toward longer wavelength and hindered charge recombination.
\nAlthough single metal doped and non-metal doped TiO2 have exhibited excellent performance in decreasing the electrons and holes recombination, but they suffer from thermal stability and losing a number of dopants during catalyst preparation process [77]. Therefore, co-doping of two kinds of atoms into TiO2 has recently attracted much interest [78]. The electronic structure of TiO2 can be altered by co-doping on TiO2 by formation of new doping levels inside its band gap. Abdullah et al. [77] reported that the doping levels situated within the band gap of TiO2 can either accept photogenerated electrons from TiO2 valence band or absorb photons with longer wavelengths. Therefore, suggesting that the TiO2 absorption range can be expanded.
\nZang et al. [79] evaluated the photocatalytic degradation of atrazine under UV and visible light irradiation by N,F-codoped TiO2 nanowires and nanoparticles in aqueous phase. It was found that photocatalytic degradation of atrazine was higher in the presence of N,F-codoped TiO2 nanowires than that of N,F-codoped TiO2 nanoparticles. The higher photocatalytic performance in the presence of N,F-codoped TiO2 nanowires was attributed to the higher charge carrier mobility and lower carrier recombination rate. Moreover, the speed of electron diffusion across nanoparticle intersections is several orders of magnitude smaller compared to that of nanowire because of frequent electron trapping at the intersections of nanoparticles and increasing the recombination of separated charges before they reach the TiO2 nanoparticles surface. Park et al. [80] showed the best performance for novel Cu/N-doped TiO2 photoelectrodes for dye-sensitized solar cells. It was found that the Cu/N-doped TiO2 nanoparticles provided higher surface area, active charge transfer and decreased charge recombination. Moreover, the addition of suitable content of Cu- to N-doped TiO2 electrode effectively inhibited the growth of TiO2 nanoparticles and improved the optical response of the photoelectrode under visible light irradiation. Chatzitakis et al. [81] studied the photoelectrochemical properties of C, N, F codoped TiO2 nanotubes. It was found that increasing surface area is not followed by increase in the photoconversion efficiency, but rather that an optimal balance between electroactive surface area and charge carrier concentration occurs.
\nZhao et al. [82] investigated the photocatalytic H2 evolution performance of Ir-C-N tridoped TiO2 under UV-visible light irradiation. The photocatalytic activity of TiO2 nanoparticles was reported to be improved by Ir-C-N tridoped TiO2 under UV-visible light, due the synergistic effect between Ir, C and N on the electron structure of TiO2. It was found that Ir existed as Ir4+ by substituting Ti in the lattice of TiO2 nanoparticles, whereas the C and N were also incorporated into the surface of TiO2 nanoparticles in interstitial mode. The absorption of TiO2 nanoparticles was expanded into the visible light region and the band gap was narrowed to ~3.0 eV, resulting in improved photocatalytic H2 evolution under UV-visible light irradiation. Tan et al. [83] investigated the photocatalytic degradation of methylene blue by W–Bi–S-tridoped TiO2 nanoparticles. It was found that the absorption edge of TiO2 was expanded into visible-light region after doping with W, Bi and S and the catalytst showed the best photocatalytic activity, than that of TiO2, S-TiO2, W–S–TiO2 and Bi–S–TiO2. This might be attributed to the synergistic effect of W, Bi and S.
\nAmongst the various strategies that have been used to enhance TiO2 photocatalytic activity, improvement of morphology, crystal structure and surface area have also been considered important and widely investigated approach to achieve better photocatalytic performance. The nanotitania crystallinity can simply be enhanced by optimizing the annealing temperature. However, the stability of the structure and geometries have to be considered when annealing [84]. For the nanotitania morphology and surface area, various ordered structures have been studied. TiO2 nanotubes [85, 86], nanowires [79], nanospheres [87], etc. Tang et al. fabricated monodisperse mesoporous anatase TiO2 nanospheres using a template material and found the resulting catalysts to show high photocatalytic degradation efficiency and selectivity towards different target dye molecules and could be readily separated from a slurry system after photocatalytic reaction [87]. Anodic TiO2 nanotubes have been reported to allow a high control over the separation of photogenerated charge carriers in photocatalytic reactions. The nanotube array has as key advantage the fact that nanotube modifications can be embedded site specifically into the tube wall or at defined locations along the tube wall. This allows for engineering of reaction sites giving rise to enhanced photocatalytic efficiencies and selectivities [88].
\nThe design and preparation of graphene-based composites containing metal oxides and metal nanoparticles have attracted attention for photocatalytic performances. For example, Tan et al. [89] prepared a novel graphene oxide-doped-oxygen-rich TiO2 (GO–OTiO2) hybrid heterostructure and evaluated its activity for photoreduction of CO2 under the irradiation of low-power energy-saving daylight bulbs. It was found that the photostability of O2–TiO2 was significantly improved by the addition of GO, at which the resulting hybrid composite retained a high reactivity. The photoactivity attained was about 1.6 and 14.0 folds higher than that of bare O2–TiO2 and the commercial Degussa P25, respectively. This high photocatalytic performance of GO–OTiO2 was attributed to the synergistic effect of the visible-light-responsiveness of O2–TiO2 and an enhanced separation and transfer of photogenerated charge carriers at the intimate interface of GO–OTiO2 heterojunctions. This study is reported to have opened up new possibilities in the development of novel, next generation heterojunction photocatalysts for energy and environmental related applications. Lin et al. [90] also investigated photoreduction of CO2 with H2O vapor in the gas-phase under the irradiation of a Xe lamp using TiO2/nitrogen (N) doped reduced graphene oxide (TiO2/NrGO) nanocomposites. They found that the quantity and configuration of N dopant in the TiO2/NrGO nanocomposites strongly influenced the photocatalytic efficiency, and the highest catalytic activity was observed for TiO2/NrGO nanocomposites with the highest N doping content. Moreover, modified TiO2/rGO demonstrated a synergistic effect, enhancing CO2 adsorption on the catalyst surface and promoting photogenerated electron transfer that resulted in a higher CO2 photoreduction rate of TiO2/NrGO. Qu et al. [91] prepared the graphene quantum dots (GQDs) with high quantum yield (about 23.6% at an excitation wavelength of 320 nm) and GQDs/TiO2 nanotubes (GQDs/TiO2 nanoparticles) nanocomposites and the photocatalytic activity was tested towards the degradation of methyl orange. It was found that the GQDs deposited on TiO2 nanoparticles can expand the visible light absorption of TiO2 nanoparticles and enhance the activity on photocatalytic degradation of methyl orange under UV-vis light irradiation (ʎ = 380–780 nm). Furthermore, the photocatalytic activity of GQDs/TiO2 nanoparticles was approximately 2.7 times as higher than that of bare TiO2 nanoparticles. Tian et al. [92] reported the preparation of N, S co-doped graphene quantum dots (N, S-GQDs)-reduced graphene oxide- (rGO)-TiO2 nanotubes (TiO2NT) nanocomposites for photodegradation of methyl orange under visible light irradiation. It was found that the S-GQDs+rGO + TiO2 nanocomposites simultaneously showed an extended photoresponse range, improved charge separation and transportation properties. Moreover, the apparent rate constant of N, S-GQDs+rGO + TiO2NT is 1.8 and 16.3 times higher compared to rGO + TiO2NT and pure TiO2NT, respectively. Suggesting that GQDs can improve the utilization of solar light for energy conversion and environmental therapy.
\nAnother drawback of TiO2 nanoparticles mentioned above is the formation of uniform suspension in water which makes its recovery difficult, therefore hindering the application of photocatalytic in an industrial scale. As a result, many studies have attempted the modification of TiO2 nanoparticles on support materials such as clays [93, 94] quartz [95], stainless steel [96], etc. Clays have been reported to be a significant support material for TiO2 nanoparticles because of their layered morphology, chemical as well as mechanical stability, cation exchange capacity, non-toxic nature, low cost and availability. Therefore, TiO2/clay nanocomposites have attracted much attention for application in both water and air purification and have been prepared by numerous researchers. Belver et al. [97] investigated the removal of atrazine under solar light using a novel W-TiO2/clay photocatalysts. It was found that the photocatalytic activity of W-TiO2/clay catalyst exhibited higher photocatalytic performance than that of an un-doped TiO2/clay, which was explained by the presence of W ions in the TiO2 nanostructure. The substitution of Ti ions with W resulted in the increase of its crystal size and the distortion of its lattice and moderately narrower band gap of photocatalysts. Mishra et al. [98] reported the preparation of TiO2/clay nanocomposites for photocatalytic degradation of VOC and dye. They found that the photocatalytic performance of TiO2/clay nanocomposites is highly dependent on the clay texture (as 2:1 clays show highest activity than 1:1) apart from their surface area and porosity. Moreover, the reactions involving TiO2/Clay photocatalyst were fast with rate constant of 0.02886 and 0.04600 min−1 for dye and VOC respectively than the other nanocomposites.
\nIn this chapter, we have given an overview of the development of modified TiO2 catalysts and its future prospects from a scientific point of view. We note that the field has experienced major advances in the last 5 years especially in the area of modifying TiO2 with carbon nanomaterials. Based on the literature we have covered here, we believe that there is still quite a lot that can be achieved in improving the performance of TiO2 catalysts for photocatalytic applications.
\nThere are no conflicts of interest to declare.
"I work with IntechOpen for a number of reasons: their professionalism, their mission in support of Open Access publishing, and the quality of their peer-reviewed publications, but also because they believe in equality. Throughout the world, we are seeing progress in attracting, retaining, and promoting women in STEMM. IntechOpen are certainly supporting this work globally by empowering all scientists and ensuring that women are encouraged and enabled to publish and take leading roles within the scientific community." Dr. Catrin Rutland, University of Nottingham, UK
",metaTitle:"Advantages of Publishing with IntechOpen",metaDescription:"We have more than a decade of experience in Open Access publishing. \n\n ",metaKeywords:null,canonicalURL:null,contentRaw:'[{"type":"htmlEditorComponent","content":"We have more than a decade of experience in Open Access publishing. The advantages of publishing with IntechOpen include:
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\n\n"In developing countries until now, advancement in science has been very limited, because insufficient economic resources are dedicated to science and education. These limitations are more marked when the scientists are women. In order to develop science in the poorest countries and decrease the gender gap that exists in scientific fields, Open Access networks like IntechOpen are essential. Free access to scientific research could contribute to ameliorating difficult life conditions and breaking down barriers." Marquidia Pacheco, National Institute for Nuclear Research (ININ), Mexico
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Today his focus is on defining the growth and development strategy for the company.",institutionString:null,institution:{name:"TU Wien",country:{name:"Austria"}}},{id:"19816",title:"Prof.",name:"Alexander",middleName:null,surname:"Kokorin",slug:"alexander-kokorin",fullName:"Alexander Kokorin",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/19816/images/1607_n.jpg",biography:"Alexander I. Kokorin: born: 1947, Moscow; DSc., PhD; Principal Research Fellow (Research Professor) of Department of Kinetics and Catalysis, N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow.\r\nArea of research interests: physical chemistry of complex-organized molecular and nanosized systems, including polymer-metal complexes; the surface of doped oxide semiconductors. 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