Metal ion vs. log βMY values.
\\n\\n
Released this past November, the list is based on data collected from the Web of Science and highlights some of the world’s most influential scientific minds by naming the researchers whose publications over the previous decade have included a high number of Highly Cited Papers placing them among the top 1% most-cited.
\\n\\nWe wish to congratulate all of the researchers named and especially our authors on this amazing accomplishment! We are happy and proud to share in their success!
\\n"}]',published:!0,mainMedia:null},components:[{type:"htmlEditorComponent",content:'IntechOpen is proud to announce that 179 of our authors have made the Clarivate™ Highly Cited Researchers List for 2020, ranking them among the top 1% most-cited.
\n\nThroughout the years, the list has named a total of 252 IntechOpen authors as Highly Cited. Of those researchers, 69 have been featured on the list multiple times.
\n\n\n\nReleased this past November, the list is based on data collected from the Web of Science and highlights some of the world’s most influential scientific minds by naming the researchers whose publications over the previous decade have included a high number of Highly Cited Papers placing them among the top 1% most-cited.
\n\nWe wish to congratulate all of the researchers named and especially our authors on this amazing accomplishment! We are happy and proud to share in their success!
\n'}],latestNews:[{slug:"intechopen-authors-included-in-the-highly-cited-researchers-list-for-2020-20210121",title:"IntechOpen Authors Included in the Highly Cited Researchers List for 2020"},{slug:"intechopen-maintains-position-as-the-world-s-largest-oa-book-publisher-20201218",title:"IntechOpen Maintains Position as the World’s Largest OA Book Publisher"},{slug:"all-intechopen-books-available-on-perlego-20201215",title:"All IntechOpen Books Available on Perlego"},{slug:"oiv-awards-recognizes-intechopen-s-editors-20201127",title:"OIV Awards Recognizes IntechOpen's Editors"},{slug:"intechopen-joins-crossref-s-initiative-for-open-abstracts-i4oa-to-boost-the-discovery-of-research-20201005",title:"IntechOpen joins Crossref's Initiative for Open Abstracts (I4OA) to Boost the Discovery of Research"},{slug:"intechopen-hits-milestone-5-000-open-access-books-published-20200908",title:"IntechOpen hits milestone: 5,000 Open Access books published!"},{slug:"intechopen-books-hosted-on-the-mathworks-book-program-20200819",title:"IntechOpen Books Hosted on the MathWorks Book Program"},{slug:"intechopen-s-chapter-awarded-the-guenther-von-pannewitz-preis-2020-20200715",title:"IntechOpen's Chapter Awarded the Günther-von-Pannewitz-Preis 2020"}]},book:{item:{type:"book",id:"230",leadTitle:null,fullTitle:"New Frontiers in Tectonic Research - General Problems, Sedimentary Basins and Island Arcs",title:"New Frontiers in Tectonic Research",subtitle:"General Problems, Sedimentary Basins and Island Arcs",reviewType:"peer-reviewed",abstract:"This book is devoted to different aspects of tectonic research. Syntheses of recent and earlier works, combined with new results and interpretations, are presented in this book for diverse tectonic settings. Most of the chapters include up-to-date material of detailed geological investigations, often combined with geophysical data, which can help understand more clearly the essence of mechanisms of different tectonic processes. Some chapters are dedicated to general problems of tectonics. Another block of chapters is devoted to sedimentary basins and special attention in this book is given to tectonic processes on active plate margins.",isbn:null,printIsbn:"978-953-307-595-2",pdfIsbn:"978-953-51-4482-3",doi:"10.5772/753",price:139,priceEur:155,priceUsd:179,slug:"new-frontiers-in-tectonic-research-general-problems-sedimentary-basins-and-island-arcs",numberOfPages:368,isOpenForSubmission:!1,isInWos:1,hash:"47476e3e55fc938c7abead3accf1d4a1",bookSignature:"Evgenii V. 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Venkateswarlu",coverURL:"https://cdn.intechopen.com/books/images_new/371.jpg",editedByType:"Edited by",editors:[{id:"58592",title:"Dr.",name:"Arun",surname:"Shanker",slug:"arun-shanker",fullName:"Arun Shanker"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"878",title:"Phytochemicals",subtitle:"A Global Perspective of Their Role in Nutrition and Health",isOpenForSubmission:!1,hash:"ec77671f63975ef2d16192897deb6835",slug:"phytochemicals-a-global-perspective-of-their-role-in-nutrition-and-health",bookSignature:"Venketeshwer Rao",coverURL:"https://cdn.intechopen.com/books/images_new/878.jpg",editedByType:"Edited by",editors:[{id:"82663",title:"Dr.",name:"Venketeshwer",surname:"Rao",slug:"venketeshwer-rao",fullName:"Venketeshwer Rao"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"4816",title:"Face Recognition",subtitle:null,isOpenForSubmission:!1,hash:"146063b5359146b7718ea86bad47c8eb",slug:"face_recognition",bookSignature:"Kresimir Delac and Mislav Grgic",coverURL:"https://cdn.intechopen.com/books/images_new/4816.jpg",editedByType:"Edited by",editors:[{id:"528",title:"Dr.",name:"Kresimir",surname:"Delac",slug:"kresimir-delac",fullName:"Kresimir Delac"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}}]},chapter:{item:{type:"chapter",id:"72527",title:"Molecular Basis of DNA Repair Defects in FUS-Associated ALS: Implications of a New Paradigm and Its Potential as Therapeutic Target",doi:"10.5772/intechopen.92637",slug:"molecular-basis-of-dna-repair-defects-in-fus-associated-als-implications-of-a-new-paradigm-and-its-p",body:'The FUS/TLS (Fused in sarcoma Protein/Translocated in liposarcoma) gene encodes a 526-amino acid protein that belongs to the TET (TAF15, EWS, and TLS) family, which is implicated in multiple aspects of RNA metabolism. The FUS gene was initially identified as an oncogene in multiple cancers. FUS fuses with the transcription repressor C/EBP homologous protein 10 (CHOP) in myxoid liposarcomas. It was identified for its role as an activator of ETS-related gene (ERG) in acute myeloid leukemia [1, 2] and in Ewing’s sarcoma tumors [3]. Subsequently, mutations in FUS were linked to motor neuron diseases, amyotrophic lateral sclerosis (ALS), and frontotemporal dementia (FTD) [4, 5].
FUS protein is ubiquitously expressed in both the nucleus and cytoplasm of many cell types; however, it is predominantly found in the nucleus of glial cells and neurons in the central nervous system. A small fraction of FUS shuttles between the nucleus and cytoplasm under various stimuli, for example, sodium arsenite-induced oxidative stress [6, 7]. A previous study revealed that FUS binds RNA in vivo to engage in nucleo-cytoplasmic shuttling [8]. Another study showed that FUS is localized to dendritic spines as an RNA-protein complex and associates with mRNA encoding an actin-stabilizer protein, which indicates a regulatory role of FUS in actin/cytoskeleton processes in dendrites [9]. Interestingly, in response to stress-induced by sorbitol, FUS redistributes to the cytoplasm and localizes to cytoplasmic stress granules [10], a complex comprised of mRNA, ribosomes, RNA-binding proteins, transcription factors and nucleases that form in response to induced stress, such as oxidative stress and heat shock to maintain the stability of selected mRNAs and protein activities [11, 12]. The redistribution of FUS on stress granules is regulated by posttranslational modification, methylation, and highly related with cell survival from the stress [10]. FUS protein contains an SYGQ-rich region at its N terminal, followed by a RGG box (RGG1), an RRM motif, a second RGG box (RGG2), a zinc finger (ZnF) motif, and a third RGG box (RGG3). The C-terminus contains a nonclassical nuclear localization signal (NLS) with conserved proline and tyrosine residues (PY-NLS). The 13 terminal amino acids (514–526) containing the NLS sequence were shown to be necessary, but not sufficient, for nuclear import of FUS [13]. FUS can bind with RNA and both single-stranded (ss) as well as double-stranded (ds) DNA [14]. FUS is associated with multiple roles in RNA processing, including splicing, transcription, and transport. Studies have highlighted that FUS has a transcriptional regulatory role in global or specialized components of transcriptional machinery [15]. A Clip-seq based study revealed that FUS regulates alternative splicing of pre-mRNAs and processing of long-intron containing transcripts, and the RNAs targeted by FUS are associated with neurogenesis and gene expression regulation; interestingly, some of FUS’ mRNA targets are involved in DNA damage response and repair pathways [16].
The prevalence of ALS has been observed to be non-uniform geographically but ranges between 0.6 and 3.8 per 100,000 population worldwide. The rate of ALS incidence appears to be rising according to the recent epidemiological studies, despite the geographical differences [17]. Notably, the incidence and prevalence of ALS are greater in men than in women [18]. It has been reported that the male: female ratio is between 1 and 3 and changes in an age-dependent manner [19]. In approximately 90% of ALS cases the cause is unknown, and, as such, they are considered sporadic (SALS); while, around 10% of ALS patients have a clear family history (FALS). In 2009, two independent studies identified that FUS R521 is mutated in FALS cases and that mutation is characterized pathologically with enhanced cytoplasmic inclusions of FUS and motor neuron degeneration [4, 5]. FUS mutations have also been linked to cases of SALS [20, 21, 22]. The FUS gene is composed of 15 exons and most mutations are clustered in exon15. Exon15 encodes the NLS domain, implying a possible involvement of its nuclear import defects. These mutations/truncations include 495X, R521C/G/H/L/S, R522G, P525L, and so on. R521 is the most commonly mutated site in ALS, whereas P525 mutations are highly related with early onset and severe progress of ALS [23, 24, 25]. Mutations also occur in domains other than NLS. For example, G187S within Gly-rich domain, G399V in RGG domain, and P431L in ZnF domain [26], which is believed to induce functional defects of FUS. Autosomal dominant mutations in the gene encoding the FUS protein have been detected in approximately 5% of FALS patients and a small subset (~1%) of SALS cases.
It is important to note that many ALS patients (36–51%) also exhibit cognitive impairment, with about 20% developing FTD, also called frontotemporal lobar degeneration (FTLD) [27], a disorder characterized by cognitive, behavioral, and linguistic dysfunction. The reverse is also seen, wherein patients with FTD can develop ALS [28]. FTD accounts for 10–15% of dementias, making it the second most common type of dementia for people under the age of 65, after Alzheimer’s disease. The overlap between ALS and FTD indicates a likely common molecular basis between FUS and cognitive deficits. After the discovery of FUS mutation in ALS, a novel subtype of FTD with FUS pathology was identified, although no FUS mutation was seen [29]. In 2010, Oriane Broustal et al. identified three exonic FUS variants, c. 1562G > A (p.Arg521His), c. 1566G > A (p.Arg522Arg), and c.188A > G (pAsn63Ser) from 317 patients including 144 patients with familial FTD and 173 patients with FTD-ALS. Interestingly, the three variants were found only in patients with both FTD and ALS [27].
The molecular mechanisms of FUS-ALS are complex and ambiguous, typically described by both loss of function and gain of toxicity hypotheses. Although controversial, loss of function is not entirely supported by animal models: FUS knockout mice and zebrafish do not develop ALS-like phenotypes [30, 31, 32]. As mentioned in the previous section, FUS plays multiple roles in RNA metabolism. In fact, thousands of RNA targets have been identified that bind to FUS in various cell lines and brain tissue from both patients and animal models [33]. The dysregulation and disturbance of RNA processing are considered to be one mechanism that leads to neurodegeneration. Depletion of FUS in mouse nervous system has been shown to alter the levels of splicing of over 950 mRNAs [34]; FUS knockout in neuroblastoma cells disturbs the splicing of more than 400 introns [35]. Expression of FUS P525L mutant was shown to inhibit splicing of minor introns by trapping U11 and U12 small nuclear RNAs (snRNAs) in these aggregates [35], and expression of R521G and R522G mutations influence RNA transcription and splicing but in a different way [36]. Besides, mRNA transport and stabilization are also affected by ALS-linked FUS mutations [37, 38].
The majority of the mutations occur in the NLS region of FUS, which induces its cytoplasmic accumulation. The widespread FUS mislocalization has been considered a hallmark of ALS [39]. Mutant, but not the wild-type FUS was shown to be assembled into stress granules in cytoplasm in response to oxidative stress or heat shock [7, 40], which potentially contributes to neurotoxicity by impairing mRNA translation [41, 42]. In fact, mutations in RNA-binding proteins (RBPs) are highly related to ALS. The interaction between mistranslocated FUS and other RBPs was recently investigated. These studies show that the cytoplasmic mislocalization caused by FUS P525L mutation impairs its interaction with other ALS-associated RBPs including shnRNPA1, hnRNPA2B1, EWSR1, and TAF15, which facilitates the nucleation of toxic cytoplasmic FUS aggregates. In addition, high cytoplasmic FUS levels exhibit defects in protein degradation and reduced protein levels of RBPs, shedding lights on the FUS-ALS pathology linked to the homeostasis of multiple ALS-associated RBPs [43].
In addition to RNA dysregulation, there has been a lot of focus on the genome instability caused by FUS mutation in ALS patients since FUS was first linked to DNA damage repair by multiple studies. In human cells, one major source of genome damage is the reactive oxygen species (ROS) accumulation-induced oxidative stress. ROS that defined as a group of reactive molecules derived from oxygen including but not limited to free radicals (superoxide, O2−), hydroxyl radical (·OH), or non-radicals (hydrogen peroxide) can be balanced by various antioxidant systems, while the imbalance between ROS production and antioxidant defenses causes oxidative stress, leading to oxidation of lipid, protein, and DNA in cells [44]. Accumulation of oxidative DNA damge has been linked to multiple neurodegenerative diseases like Parkinson’s disease (PD) and Huntington’s disease (HD) [45, 46]. In addition to DNA damage, mutation in the genes of specific DNA repair pathways that lead to DNA damage repair (DDR) is another challenge for the central nervous system [47]. For example, nucleotide excision repair (NER) is defective in xeroderma pigmentosum (XP) and Cockayne syndrome (CS), base excision/single-strand break repair (BER/SSBR) defects in ataxia with oculomotor apraxia type 1 (AOA1) [48], spinocerebellar ataxia with axonal neuropathy (SCAN1) [49] and ALS [50], and defective DDR signaling and DNA double-strand break repair (DSBR) in ataxia telangiectasia (A-T) and Nijmegen break-age syndrome. FUS is found to be phosphorylated by DDR proteins ataxia-telangiectasia mutated (ATM) and DNA-dependent protein kinase (DNA-PK) in response to DSB-inducing agents. FUS was identified to interact with histone deacetylase 1 (HDAC1) in primary mouse cortical neurons, and the interaction is believed to modulate the homologous recombination (HR) and non-homologous end joining (NHEJ), two major pathways for DSB repair. Besides, FUS was shown to be recruited at DNA damage tracks induced by microirradiation (MIR) at wavelengths of 405 or 351 nm, in a PARP1-depedent manner and accompanied with PARylation by PARP1 [51, 52, 53]. Notably, MIR causes clusters of different types of DNA damage including oxidized base lesions, single-strand breaks (SSBs), and DSBs. It is generally believed that UVA (wavelength between 320 and 400 nm) predominantly induces SSBs via elevated ROS, while UVA may also induce secondary DSBs due to clustered SSBs [54]. Thus, recruitment of FUS at MIR with wavelength of 351 nm suggests its potential role in the repair of SSBs.
A comprehensive investigation by our group described the mechanistic role of FUS in BER/SSBR, a major pathway to repair oxidative DNA damage. Our study utilized multiple in vitro and in vivo model systems, including, CRISPR/Cas9-mediated FUS knockout (KO) human embryonic kidney (HEK)293 cells, FALS patient-derived induced pluripotent stem cells (iPSCs) with FUS mutations R521H and P525L, motor neurons induced from these iPSC lines, and ALS patients spinal cord tissues with FUS pathology. We discovered that the DNA integrity is substantially affected in the spinal cord tissues and the motor neurons derived from ALS patients. Both downregulation and pathological mutation of FUS were associated with DNA SSB accumulation and SSBR defects. Finally, we identified that FUS directly interacts with PARP1, XRCC1, and LigIII in response to oxidative stress and FUS facilitates the recruitment of XRCC1/LigIII to DNA damage sites in a PARP1 activity-dependent manner. FUS enhances the ligation activity of LigIII, which is critical for an optimal SSBR in neurons (Figure 1). The SSBR deficiency due to ALS-linked FUS mutations can be rescued by the correction of those mutations via Crisper/Cas9 technology [50]. Furthermore, FUS regulates PARP1’s PARylation activity in motor neurons and thus could affect neuronal energy metabolism by uncoupling NAD+/NADH levels.
Model of FUS involving DNA damage response in the nucleus. In response to DNA SSBs, FUS is PARylated and recruited to DNA damage sites by PARP1 and the recruitment facilitates the loading of XRCC1 and nuclear LigIII (nLigIII) complex, where FUS enhances the ligation activity of LigIII for an optimal SSB ligating. While in response to DSB, FUS is associated with HDAC1, which is required for an efficient NHEJ and HR-mediated DSB repair. FUS is also phosphorylated by ATM and DNA-PK, although the underlying mechanism is not known. Due to its role in the functional activation of LigII, which is involved in MMEJ-mediated DSB repair, it is likely that FUS also affects MMEJ, which needs to be investigated.
During DDR, PARP1 plays an important role in regulating DNA damage repair. In response to DNA damage, PARP1 is self-activated by its auto-PARylation and transfers ADP-ribose to create long and branched poly(ADP-ribose) on target DNA repair proteins to facilitate their recruitment; for example, PARP1 recruits XRCC1 by its PARylation. A study showed that PARP1 likely plays a major role for the poly(ADP-ribose) synthesis induced by alkylating agents, since the amount of poly(ADP-ribose) can be reduced for around 10 folds (from 60 pmol per mg of DNA to 5.85 pmol per mg of DNA) in PARP1 KO cells in the presence of MNNG [55], which activates DNA mismatch repair. Consistantly, PARP1 knockout mice are highly susceptible to DNA damaging agents and are accumulated with DNA strand breaks accompanied with genomic instability in them [56, 57].
In response to DNA damage, FUS is recruited to DNA damage site in a PARP1 activity-dependent manner [51, 52]. FUS directly binds to PAR synthesized by activated PARP1 leading to the formation of damaged DNA-rich compartments contributed by its N-terminal low-complexity domain (LCD) and C-terminal RGG domains, and the compartments are dissociated by the hydrolysis of PAR by PARG [58], which indicates that PAR polymers play an essential role for the recruitment, likely through enhancing the FUS droplet formation [59]. While the activation of PARP1 can induce shuttling of FUS from nucleus to cytoplasm, which in turn enhances FUS aggregate formation and neurodegeneration [58, 60]. Furthermore, like FUS, the other two members in TET family, TAF15 and EWSR1 are also recruited to MIR-induced DNA damage tracks depending on PARP1 activity [53], while the molecular mechanism of the cross-talk between TET family proteins and PARP-1 has not been investigated.
Although, recent reports from our group and others demonstrate a complex, but the direct role of FUS in maintaining genome integrity, whether FUS RNA-binding activity plays a role in regulating the expression of DDR factors has not been investigated. FUS regulates several key steps of RNA metabolism that impairs various biological processes. CLIP-seq has been used to identify RNAs that FUS targeted in multiple studies [16, 34, 61, 62, 63, 64, 65], which reveals an indirect role of FUS involving in DDR by regulating RNA transcription. One report shows that FUS regulates alternative splicing of pre-mRNAs and processing of long-intron containing transcripts in HeLa cells, and FUS binds RNA encoding proteins important for DNA damage response and repair pathways. By comparing with other CLIP-based assays, a map of FUS RNA targets to DNA DSBR by NHEJ and HR is generated in the report and in which, a number of key DDR factors such as ATM, 53BP1, MRN11, NBS1 are included [16]. We recently performed RT2 PCR arrays for DNA repair and DDR signaling pathways in CRISPR/cas9 FUS knockout (KO) cells, patient-derived FUS-mutant cells, as well as FUS-ALS patient spinal cord autopsy tissue, which revealed significant downregulation of DDR factors BRCA1, MSH complex, RAD23B, and DNA ligase 4. Notably, BRCA1 depletion has been linked to neuronal DNA DSB accumulation and cognitive defects in Alzheimer’s disease. The ubiquitin receptor RAD23 functions both in nucleotide excision repair and the proteasomal protein clearance pathway and is thus linked to amyloid load in neurodegeneration. This study provides evidence of FUS pathology-mediated perturbation in the expression of DNA repair and DDR signaling factors and thus highlights the intricate connections between FUS, genome instability, and neurodegeneration.
As early as 1982, the defective DNA repair and its possible role in ALS pathology was first proposed by Bradley et al. [66], where they hypothesize that abnormal DNA in ALS may arise from a deficiency of an isozyme of a DNA repair factor. Subsequently, growing evidence suggests that defective DNA repair is a common feature of not only ALS but also several other neurodegenerative diseases, underscoring the needs of studying the implications of unrepaired DNA damage in neurons affected by neurodegeneration [67], which may lead to novel therapeutic strategies.
Our recent studies made a critical breakthrough in this direction by first time shedding lights on the molecular insights into the involvement of ALS and FTD-associated FUS and other RNA/DNA-binding proteins in specific DNA repair failure mechanisms, such as DNA ligation deficiency. While this study suggests a potential for DNA ligase complementation strategy, several key questions should be addressed to develop DNA repair-based interventions for ALS. These are: (1) The role of FUS in mitochondrial genome stability maintaining. The linkage between FUS and mitochondrial integrity has been established by a number of studies. Deng et al. demonstrated interactions between FUS and two mitochondrial proteins, mitochondrial chaperonin HSP60 and ATP synthase beta subunit ATP5B, in different studies. HSP60 mediates the translocation of FUS into mitochondria, and downregulating of HSP60 rescues mitochondrial defects and neurodegenerative phenotypes in FUS transgenic flies. While interaction between FUS and ATP5B indicates a involvement of FUS in the dysregulation of mitochondrial ATP synthesis: expression of wild-type or FUS P525L mutant disrupts the formation of the mitochondrial ATP synthase supercomplexes and suppresses the activity of ATP synthase, resulting in mitochondrial cristae loss followed by mitochondrial fragmentation [68, 69]. Nakaya and Maragkakis et al. found that expression of human FUS R495X in mouse embryonic stem cell-differentiated neurons disturbs the translation efficiency of mitochondria-associated genes and results in significant reduction of mitochondrial size [70]. Although ALS-FUS has been linked with the dysfunction of mitochondria, the role of FUS in mitochondrial genome integrity has not been explored. (2) The role of FUS in microhomology-mediated end joining (MMEJ) repair. We have established a relationship between FUS and XRCC1/LigIII, which is required for an optimal SSBR. While LigIII, together with XRCC1 and PARP1, also participates in the MMEJ-mediated DSB repair pathway, the role of which in primary neurons is unknown (Figure 1). We hypothesized that the MMEJ contributes DSBR in motor neurons and the loss of FUS may affect MMEJ and lead to genomic instability, which we are currently pursuing. (3) The role of FUS in maintaining genome integrity in astrocytes. Recent studies have shown that expression of ALS-linked mutant FUS and other ALS causative factors in astrocytes induces motor neuron death [71, 72, 73]. It will, therefore, be critical to investigate FUS toxicity-induced ligation activity defects in astrocytes and the collateral influence on motor neurons. (4) Whether DNA ligase I (LigI) rescues FUS mutant-mediated LigIII defects. Mammalian cells express three DNA ligases including ligase IV (LigIV), LigIII, and LigI. LigIV specifically participates in NHEJ-mediated DSB repair; LigIII has nuclear and mitochondrial isoforms. Both the nuclear and mitochondrial isoforms have ~98% similarity and function in BER/single-strand break repair (SSBR); LigI has been shown to functionally overlap with LigIII and is believed a back-up of LigIII, however, the level of LigI expression in non-cycling, postmitotic cells like neurons is negligible due to lack of replication-associated repair. Very likely, the induction of LigI into motor neurons with FUS pathology can rescue the LigIII ligation activity defects caused by FUS mutation.
Addressing these critical follow-up questions is an unmet need in the FUS-ALS field, which will help to develop a mechanism-based DNA-repair-targeted therapy. With recent emerging studies, the stage is set for such a paradigm shift.
The research was supported by grants from the National Institute of Neurological Disorders and Stroke (NINDS) of the National Institute of Health (NIH) under the award numbers R01NS088645, RF1NS112719 and the Houston Methodist Research Institute funds. The content is solely the responsibility of the authors and does not necessarily represent the official views of the funding agencies.
Stability constant of the formation of metal complexes is used to measure interaction strength of reagents. From this process, metal ion and ligand interaction formed the two types of metal complexes; one is supramolecular complexes known as host-guest complexes [1] and the other is anion-containing complexes. In the solution it provides and calculates the required information about the concentration of metal complexes.
Solubility, light, absorption conductance, partitioning behavior, conductance, and chemical reactivity are the complex characteristics which are different from their components. It is determined by various numerical and graphical methods which calculate the equilibrium constants. This is based on or related to a quantity, and this is called the complex formation function.
During the displacement process at the time of metal complex formation, some ions disappear and form a bonding between metal ions and ligands. It may be considered due to displacement of a proton from a ligand species or ions or molecules causing a drop in the pH values of the solution [2]. Irving and Rossotti developed a technique for the calculation of stability constant, and it is called potentiometric technique.
To determine the stability constant, Bjerrum has used a very simple method, and that is metal salt solubility method. For the studies of a larger different variety of polycarboxylic acid-, oxime-, phenol-containing metal complexes, Martel and Calvin used the potentiometric technique for calculating the stability constant. Those ligands [3, 4] which are uncharged are also examined, and their stability constant calculations are determined by the limitations inherent in the ligand solubility method. The limitations of the metal salt solubility method and the result of solubility methods are compared with this. M-L, MLM, and (M3) L are some types of examples of metal-ligand bonding. One thing is common, and that is these entire types metal complexes all have one ligand.
The solubility method can only usefully be applied to studies of such complexes, and it is best applied for ML; in such types of system, only ML is formed. Jacqueline Gonzalez and his co-worker propose to explore the coordination chemistry of calcium complexes. Jacqueline and et al. followed this technique for evaluate the as partial model of the manganese-calcium cluster and spectrophotometric studies of metal complexes, i.e., they were carried calcium(II)-1,4-butanediamine in acetonitrile and calcium(II)-1,2-ethylendiamine, calcium(II)-1,3-propanediamine by them.
Spectrophotometric programming of HypSpec and received data allows the determination of the formation of solubility constants. The logarithmic values, log β110 = 5.25 for calcium(II)-1,3-propanediamine, log β110 = 4.072 for calcium(II)-1,4-butanediamine, and log β110 = 4.69 for calcium(II)-1,2-ethylendiamine, are obtained for the formation constants [5]. The structure of Cimetidine and histamine H2-receptor is a chelating agent. Syed Ahmad Tirmizi has examined Ni(II) cimetidine complex spectrophotometrically and found an absorption peak maximum of 622 nm with respect to different temperatures.
Syed Ahmad Tirmizi have been used to taken 1:2 ratio of metal and cimetidine compound for the formation of metal complex and this satisfied by molar ratio data. The data, 1.40–2.4 × 108, was calculated using the continuous variation method and stability constant at room temperature, and by using the mole ratio method, this value at 40°C was 1.24–2.4 × 108. In the formation of lead(II) metal complexes with 1-(aminomethyl) cyclohexene, Thanavelan et al. found the formation of their binary and ternary complexes. Glycine,
Using the stability constant method, these ternary complexes were found out, and using the parameters such as Δ log K and log X, these ternary complex data were compared with binary complex. The potentiometric technique at room temperature (25°C) was used in the investigation of some binary complex formations by Abdelatty Mohamed Radalla. These binary complexes are formed with 3D transition metal ions like Cu2+, Ni2+, Co2+, and Zn2+ and gallic acid’s importance as a ligand and 0.10 mol dm−3 of NaNO3. Such types of aliphatic dicarboxylic acids are very important biologically. Many acid-base characters and the nature of using metal complexes have been investigated and discussed time to time by researchers [7].
The above acids (gallic and aliphatic dicarboxylic acid) were taken to determine the acidity constants. For the purpose of determining the stability constant, binary and ternary complexes were carried in the aqueous medium using the experimental conditions as stated above. The potentiometric pH-metric titration curves are inferred for the binary complexes and ternary complexes at different ratios, and formation of ternary metal complex formation was in a stepwise manner that provided an easy way to calculate stability constants for the formation of metal complexes.
The values of Δ log K, percentage of relative stabilization (% R. S.), and log X were evaluated and discussed. Now it provides the outline about the various complex species for the formation of different solvents, and using the concentration distribution, these complexes were evaluated and discussed. The conductivity measurements have ascertained for the mode of ternary chelating complexes.
A study by Kathrina and Pekar suggests that pH plays an important role in the formation of metal complexes. When epigallocatechin gallate and gallic acid combine with copper(II) to form metal complexes, the pH changes its speculation. We have been able to determine its pH in frozen and fluid state with the help of multifrequency EPR spectroscopy [8]. With the help of this spectroscopy, it is able to detect that each polyphenol exhibits the formation of three different mononuclear species. If the pH ranges 4–8 for di- or polymeric complex of Cu(II), then it conjectures such metal complexes. It is only at alkaline pH values.
The line width in fluid solutions by molecular motion exhibits an incomplete average of the parameters of anisotropy spin Hamilton. If the complexes are different, then their rotational correlation times for this also vary. The analysis of the LyCEP anisotropy of the fluid solution spectra is performed using the parameters determined by the simulation of the rigid boundary spectra. Its result suggests that pH increases its value by affecting its molecular mass. It is a polyphenol ligand complex with copper, showing the coordination of an increasing number of its molecules or increasing participation of polyphenol dimers used as ligands in the copper coordination region.
The study by Vishenkova and his co-worker [8] provides the investigation of electrochemical properties of triphenylmethane dyes using a voltammetric method with constant-current potential sweep. Malachite green (MG) and basic fuchsin (BF) have been chosen as representatives of the triphenylmethane dyes [9]. The electrochemical behavior of MG and BF on the surface of a mercury film electrode depending on pH, the nature of background electrolyte, and scan rate of potential sweep has been investigated.
Using a voltammetric method with a constant-current potential sweep examines the electrical properties of triphenylmethane dye. In order to find out the solution of MG and BF, certain registration conditions have been prescribed for it, which have proved to be quite useful. The reduction peak for the currents of MG and BF has demonstrated that it increases linearly with respect to their concentration as 9.0 × 10−5–7.0 × 10−3 mol/dm3 for MG and 6.0 × 10−5–8.0 × 10−3 mol/dm3 for BF and correlation coefficients of these values are 0.9987 for MG and 0.9961 for BF [10].
5.0 × 10−5 and 2.0 × 10−5 mol/dm3 are the values used as the detection limit of MG and BF, respectively. Stability constants are a very useful technique whose size is huge. Due to its usefulness, it has acquired an umbrella right in the fields of chemistry, biology, and medicine. No science subject is untouched by this. Stability constants of metal complexes are widely used in the various areas like pharmaceuticals as well as biological processes, separation techniques, analytical processes, etc. In the presented chapter, we have tried to explain this in detail by focusing our attention on the applications and solutions of stability of metal complexes in solution.
Stability or formation or binding constant is the type of equilibrium constant used for the formation of metal complexes in the solution. Acutely, stability constant is applicable to measure the strength of interactions between the ligands and metal ions that are involved in complex formation in the solution [11]. A generally these 1-4 equations are expressed as the following ways:
Thus
K1, K2, K3, … Kn are the equilibrium constants and these are also called stepwise stability constants. The formation of the metal-ligand-n complex may also be expressed as equilibrium constants by the following steps:
The parameters K and β are related together, and these are expressed in the following example:
Now the numerator and denominator are multiplied together with the use of [metal-ligand] [metal-ligand2], and after the rearranging we get the following equation:
Now we expressed it as the following:
From the above relation, it is clear that the overall stability constant βn is equal to the product of the successive (i.e., stepwise) stability constants, K1, K2, K3,…Kn. This in other words means that the value of stability constants for a given complex is actually made up of a number of stepwise stability constants. The term stability is used without qualification to mean that the complex exists under a suitable condition and that it is possible to store the complex for an appreciable amount of time. The term stability is commonly used because coordination compounds are stable in one reagent but dissociate or dissolve in the presence of another regent. It is also possible that the term stability can be referred as an action of heat or light or compound. The stability of complex [13] is expressed qualitatively in terms of thermodynamic stability and kinetic stability.
In a chemical reaction, chemical equilibrium is a state in which the concentration of reactants and products does not change over time. Often this condition occurs when the speed of forward reaction becomes the same as the speed of reverse reaction. It is worth noting that the velocities of the forward and backward reaction are not zero at this stage but are equal.
If hydrogen and iodine are kept together in molecular proportions in a closed process vessel at high temperature (500°C), the following action begins:
In this activity, hydrogen iodide is formed by combining hydrogen and iodine, and the amount of hydrogen iodide increases with time. In contrast to this action, if the pure hydrogen iodide gas is heated to 500°C in the reaction, the compound is dissolved by reverse action, which causes hydrogen iodide to dissolve into hydrogen and iodine, and the ratio of these products increases over time. This is expressed in the following reaction:
For the formation of metal chelates, the thermodynamic technique provides a very significant information. Thermodynamics is a very useful technique in distinguishing between enthalpic effects and entropic effects. The bond strengths are totally effected by enthalpic effect, and this does not make any difference in the whole solution in order/disorder. Based on thermodynamics the chelate effect below can be best explained. The change of standard Gibbs free energy for equilibrium constant is response:
Where:
R = gas constant
T = absolute temperature
At 25°C,
ΔG = (− 5.708 kJ mol−1) · log β.
The enthalpy term creates free energy, i.e.,
For metal complexes, thermodynamic stability and kinetic stability are two interpretations of the stability constant in the solution. If reaction moves from reactants to products, it refers to a change in its energy as shown in the above equation. But for the reactivity, kinetic stability is responsible for this system, and this refers to ligand species [14].
Stable and unstable are thermodynamic terms, while labile and inert are kinetic terms. As a rule of thumb, those complexes which react completely within about 1 minute at 25°C are considered labile, and those complexes which take longer time than this to react are considered inert. [Ni(CN)4]2− is thermodynamically stable but kinetically inert because it rapidly exchanges ligands.
The metal complexes [Co(NH3)6]3+ and such types of other complexes are kinetically inert, but these are thermodynamically unstable. We may expect the complex to decompose in the presence of acid immediately because the complex is thermodynamically unstable. The rate is of the order of 1025 for the decomposition in acidic solution. Hence, it is thermodynamically unstable. However, nothing happens to the complex when it is kept in acidic solution for several days. While considering the stability of a complex, always the condition must be specified. Under what condition, the complex which is stable or unstable must be specified such as acidic and also basic condition, temperature, reactant, etc.
A complex may be stable with respect to a particular condition but with respect to another. In brief, a stable complex need not be inert and similarly, and an unstable complex need not be labile. It is the measure of extent of formation or transformation of complex under a given set of conditions at equilibrium [15].
Thermodynamic stability has an important role in determining the bond strength between metal ligands. Some complexes are stable, but as soon as they are introduced into aqueous solution, it is seen that these complexes have an effect on stability and fall apart. For an example, we take the [Co (SCN)4]2+ complex. The ion bond of this complex is very weak and breaks down quickly to form other compounds. But when [Fe(CN)6]3− is dissolved in water, it does not test Fe3+ by any sensitive reagent, which shows that this complex is more stable in aqueous solution. So it is indicated that thermodynamic stability deals with metal-ligand bond energy, stability constant, and other thermodynamic parameters.
This example also suggests that thermodynamic stability refers to the stability and instability of complexes. The measurement of the extent to which one type of species is converted to another species can be determined by thermodynamic stability until equilibrium is achieved. For example, tetracyanonickelate is a thermodynamically stable and kinetic labile complex. But the example of hexa-amine cobalt(III) cation is just the opposite:
Thermodynamics is used to express the difference between stability and inertia. For the stable complex, large positive free energies have been obtained from ΔG0 reaction. The ΔH0, standard enthalpy change for this reaction, is related to the equilibrium constant, βn, by the well thermodynamic equation:
For similar complexes of various ions of the same charge of a particular transition series and particular ligand, ΔS0 values would not differ substantially, and hence a change in ΔH0 value would be related to change in βn values. So the order of values of ΔH0 is also the order of the βn value.
Kinetic stability is referred to the rate of reaction between the metal ions and ligand proceeds at equilibrium or used for the formation of metal complexes. To take a decision for kinetic stability of any complexes, time is a factor which plays an important role for this. It deals between the rate of reaction and what is the mechanism of this metal complex reaction.
As we discuss above in thermodynamic stability, kinetic stability is referred for the complexes at which complex is inert or labile. The term “inert” was used by Tube for the thermally stable complex and for reactive complexes the term ‘labile’ used [16]. The naturally occurring chlorophyll is the example of polydentate ligand. This complex is extremely inert due to exchange of Mg2+ ion in the aqueous media.
The nature of central atom of metal complexes, dimension, its degree of oxidation, electronic structure of these complexes, and so many other properties of complexes are affected by the stability constant. Some of the following factors described are as follows.
In the coordination chemistry, metal complexes are formed by the interaction between metal ions and ligands. For these type of compounds, metal ions are the coordination center, and the ligand or complexing agents are oriented surrounding it. These metal ions mostly are the transition elements. For the determination of stability constant, some important characteristics of these metal complexes may be as given below.
Ligands are oriented around the central metal ions in the metal complexes. The sizes of these metal ions determine the number of ligand species that will be attached or ordinated (dative covalent) in the bond formation. If the sizes of these metal ions are increased, the stability of coordination compound defiantly decreased. Zn(II) metal ions are the central atoms in their complexes, and due to their lower size (0.74A°) as compared to Cd(II) size (0.97A°), metal ions are formed more stable.
Hence, Al3+ ion has the greatest nuclear charge, but its size is the smallest, and the ion N3− has the smallest nuclear charge, and its size is the largest [17]. Inert atoms like neon do not participate in the formation of the covalent or ionic compound, and these atoms are not included in isoelectronic series; hence, it is not easy to measure the radius of this type of atoms.
The properties of stability depend on the size of the metal ion used in the complexes and the total charge thereon. If the size of these metal ions is small and the total charge is high, then their complexes will be more stable. That is, their ratio will depend on the charge/radius. This can be demonstrated through the following reaction:
An ionic charge is the electric charge of an ion which is formed by the gain (negative charge) or loss (positive charge) of one or more electrons from an atom or group of atoms. If we talk about the stability of the coordination compounds, we find that the total charge of their central metal ions affects their stability, so when we change their charge, their stability in a range of constant can be determined by propagating of error [18]. If the charge of the central metal ion is high and the size is small, the stability of the compound is high:
In general, the most stable coordination bonds can cause smaller and highly charged rations to form more stable coordination compounds.
When an electron pair attracts a central ion toward itself, a strong stability complex is formed, and this is due to electron donation from ligand → metal ion. This donation process is increasing the bond stability of metal complexes exerted the polarizing effect on certain metal ions. Li+, Na+, Mg2+, Ca2+, Al3+, etc. are such type of metal cation which is not able to attract so strongly from a highly electronegative containing stable complexes, and these atoms are O, N, F, Au, Hg, Ag, Pd, Pt, and Pb. Such type of ligands that contains P, S, As, Br and I atom are formed stable complex because these accepts electron from M → π-bonding. Hg2+, Pb2+, Cd2+, and Bi3+ metal ions are also electronegative ions which form insoluble salts of metal sulfide which are insoluble in aqueous medium.
Volatile ligands may be lost at higher temperature. This is exemplified by the loss of water by hydrates and ammonia:
The transformation of certain coordination compounds from one to another is shown as follows:
A ligand is an ion or small molecule that binds to a metal atom (in chemistry) or to a biomolecule (in biochemistry) to form a complex, such as the iron-cyanide coordination complex Prussian blue or the iron-containing blood-protein hemoglobin. The ligands are arranged in spectrochemical series which are based on the order of their field strength. It is not possible to form the entire series by studying complexes with a single metal ion; the series has been developed by overlapping different sequences obtained from spectroscopic studies [19]. The order of common ligands according to their increasing ligand field strength is
The above spectrochemical series help us to for determination of strength of ligands. The left last ligand is as weaker ligand. These weaker ligand cannot forcible binding the 3d electron and resultant outer octahedral complexes formed. It is as-
Increasing the oxidation number the value of Δ increased.
Δ increases from top to bottom.
However, when we consider the metal ion, the following two useful trends are observed:
Δ increases with increasing oxidation number.
Δ increases down a group. For the determination of stability constant, the nature of the ligand plays an important role.
The following factors described the nature of ligands.
The size and charge are two factors that affect the production of metal complexes. The less charges and small sizes of ligands are more favorable for less stable bond formation with metal and ligand. But if this condition just opposite the product of metal and ligand will be a more stable compound. So, less nuclear charge and more size= less stable complex whereas if more nuclear charge and small in size= less stable complex. We take fluoride as an example because due to their smaller size than other halide and their highest electro negativity than the other halides formed more stable complexes. So, fluoride ion complexes are more stable than the other halides:
As compared to S2− ion, O22− ions formed more stable complexes.
It is suggested by Calvin and Wilson that the metal complexes will be more stable if the basic character or strength of ligands is higher. It means that the donating power of ligands to central metal ions is high [20].
It means that the donating power of ligands to central metal ions is high. In the case of complex formation of aliphatic diamines and aromatic diamines, the stable complex is formed by aliphatic diamines, while an unstable coordination complex is formed with aromatic diamines. So, from the above discussion, we find that the stability will be grater if the e-donation power is greater.
Thus it is clear that greater basic power of electron-donating species will form always a stable complex. NH3, CN−, and F− behaved as ligands and formed stable complexes; on the other hand, these are more basic in nature.
We know that if the concentration of coordination group is higher, these coordination compounds will exist in the water as solution. It is noted that greater coordinating tendency show the water molecules than the coordinating group which is originally present. SCN− (thiocynate) ions are present in higher concentration; with the Co2+ metal ion, it formed a blue-colored complex which is stable in state, but on dilution of water medium, a pink color is generated in place of blue, or blue color complex is destroyed by [Co(H2O)6]2+, and now if we added further SCN−, the pink color will not appear:
Now it is clear that H2O and SCN− are in competition for the formation of Co(II) metal-containing complex compound. In the case of tetra-amine cupric sulfate metal complex, ammonia acts as a donor atom or ligand. If the concentration of NH3 is lower in the reaction, copper hydroxide is formed but at higher concentration formed tetra-amine cupric sulfate as in the following reaction:
For a metal ion, chelating ligand is enhanced and affinity it and this is known as chelate effect and compared it with non-chelating and monodentate ligand or the multidentate ligand is acts as chelating agent. Ethylenediamine is a simple chelating agent (Figure 1).
Structure of ethylenediamine.
Due to the bidentate nature of ethylenediamine, it forms two bonds with metal ion or central atom. Water forms a complex with Ni(II) metal ion, but due to its monodentate nature, it is not a chelating ligand (Figures 2 and 3).
Structure of chelating configuration of ethylenediamine ligand.
Structure of chelate with three ethylenediamine ligands.
The dentate cheater of ligand provides bonding strength to the metal ion or central atom, and as the number of dentate increased, the tightness also increased. This phenomenon is known as chelating effect, whereas the formation of metal complexes with these chelating ligands is called chelation:
or
Some factors are of much importance for chelation as follows.
The sizes of the chelating ring are increased as well as the stability of metal complex decreased. According to Schwarzenbach, connecting bridges form the chelating rings. The elongated ring predominates when long bridges connect to the ligand to form a long ring. It is usually observed that an increased a chelate ring size leads to a decrease in complex stability.
He interpreted this statement. The entropy of complex will be change if the size of chelating ring is increased, i.e., second donor atom is allowed by the chelating ring. As the size of chelating ring increased, the stability should be increased with entropy effect. Four-membered ring compounds are unstable, whereas five-membered are more stable. So the chelating ring increased its size and the stability of the formed metal complexes.
The number of chelating rings also decides the stability of complexes. Non-chelating metal compounds are less stable than chelating compounds. These numbers increase the thermodynamic volume, and this is also known as an entropy term. In recent years ligands capable of occupying as many as six coordination positions on a single metal ion have been described. The studies on the formation constants of coordination compounds with these ligands have been reported. The numbers of ligand or chelating agents are affecting the stability of metal complexes so as these numbers go up and down, the stability will also vary with it.
For the Ni(II) complexes with ethylenediamine as chelating agent, its log K1 value is 7.9 and if chelating agents are trine and penten, then the log K1 values are 7.9 and 19.3, respectively. If the metal ion change Zn is used in place of Ni (II), then the values of log K1 for ethylenediamine, trine, and penten are 6.0, 12.1, and 16.2, respectively. The log βMY values of metal ions are given in Table 1.
Metal ion | log βMY (25°C, I = 0.1 M) |
---|---|
Ca2+ | 11.2 |
Cu2+ | 19.8 |
Fe3+ | 24.9 |
Metal ion vs. log βMY values.
Ni(NH3)62+ is an octahedral metal complex, and at 25 °C its log β6 value is 8.3, but Ni(ethylenediamine)32+ complex is also octahedral in geometry, with 18.4 as the value of log β6. The calculated stability value of Ni(ethylenediamine)32+ 1010 times is more stable because three rings are formed as chelating rings by ethylenediamine as compared to no such ring is formed. Ethylenediaminetetraacetate (EDTA) is a hexadentate ligand that usually formed stable metal complexes due to its chelating power.
A special effect in molecules is when the atoms occupy space. This is called steric effect. Energy is needed to bring these atoms closer to each other. These electrons run away from near atoms. There can be many ways of generating it. We know the repulsion between valence electrons as the steric effect which increases the energy of the current system [21]. Favorable or unfavorable any response is created.
For example, if the static effect is greater than that of a product in a metal complex formation process, then the static increase would favor this reaction. But if the case is opposite, the skepticism will be toward retardation.
This effect will mainly depend on the conformational states, and the minimum steric interaction theory can also be considered. The effect of secondary steric is seen on receptor binding produced by an alternative such as:
Reduced access to a critical group.
Stick barrier.
Electronic resonance substitution bond by repulsion.
Population of a conformer changes due to active shielding effect.
The macrocyclic effect is exactly like the image of the chelate effect. It means the principle of both is the same. But the macrocyclic effect suggests cyclic deformation of the ligand. Macrocyclic ligands are more tainted than chelating agents. Rather, their compounds are more stable due to their cyclically constrained constriction. It requires some entropy in the body to react with the metal ion. For example, for a tetradentate cyclic ligand, we can use heme-B which forms a metal complex using Fe+2 ions in biological systems (Figure 4).
Structure of hemoglobin is the biological complex compound which contains Fe(II) metal ion.
The n-dentate chelating agents play an important role for the formation of more stable metal complexes as compared to n-unidentate ligands. But the n-dentate macrocyclic ligand gives more stable environment in the metal complexes as compared to open-chain ligands. This change is very favorable for entropy (ΔS) and enthalpy (ΔH) change.
There are so many parameters to determination of formation constants or stability constant in solution for all types of chelating agents. These numerous parameters or techniques are refractive index, conductance, temperature, distribution coefficients, refractive index, nuclear magnetic resonance volume changes, and optical activity.
Solubility products are helpful and used for the insoluble salt that metal ions formed and complexes which are also formed by metal ions and are more soluble. The formation constant is observed in presence of donor atoms by measuring increased solubility.
To determine the solubility constant, it involves the distribution of the ligands or any complex species; metal ions are present in two immiscible solvents like water and carbon tetrachloride, benzene, etc.
In this method metal ions or ligands are present in solution and on exchanger. A solid polymers containing with positive and negative ions are ion exchange resins. These are insoluble in nature. This technique is helpful to determine the metal ions in resin phase, liquid phase, or even in radioactive metal. This method is also helpful to determine the polarizing effect of metal ions on the stability of ligands like Cu(II) and Zn(II) with amino acid complex formation.
At the equilibrium free metal and ions are present in the solution, and using the different electrometric techniques as described determines its stability constant.
This method is based upon the titration method or follows its principle. A stranded acid-base solution used as titrate and which is titrated, it may be strong base or strong acid follows as potentiometrically. The concentration of solution using 103− M does not decomposed during the reaction process, and this method is useful for protonated and nonprotonated ligands.
This is the graphic method used to determine the stability constant in producing metal complex formation by plotting a polarograph between the absences of substances and the presence of substances. During the complex formation, the presence of metal ions produced a shift in the half-wave potential in the solution.
If a complex is relatively slow to form and also decomposes at measurable rate, it is possible, in favorable situations, to determine the equilibrium constant.
This involves the study of the equilibrium constant of slow complex formation reactions. The use of tracer technique is extremely useful for determining the concentrations of dissociation products of the coordination compound.
This method is based on the study of the effect of an equilibrium concentration of some ions on the function at a definite organ of a living organism. The equilibrium concentration of the ion studied may be determined by the action of this organ in systems with complex formation.
The solution of 25 ml is adopted by preparing at the 1.0 × 10−5 M ligand or 1.0 × 10−5 M concentration and 1.0 × 10−5 M for the metal ion:
The solutions containing the metal ions were considered both at a pH sufficiently high to give almost complete complexation and at a pH value selected in order to obtain an equilibrium system of ligand and complexes.
In order to avoid modification of the spectral behavior of the ligand due to pH variations, it has been verified that the range of pH considered in all cases does not affect absorbance values. Use the collected pH values adopted for the determinations as well as selected wavelengths. The ionic strengths calculated from the composition of solutions allowed activity coefficient corrections. Absorbance values were determined at wavelengths in the range 430–700 nm, every 2 nm.
For a successive metal complex formation, use this method. If ligand is protonate and the produced complex has maximum number of donate atoms of ligands, a selective light is absorbed by this complex, while for determination of stability constant, it is just known about the composition of formed species.
Bjerrum (1941) used the method stepwise addition of the ligands to coordination sphere for the formation of complex. So, complex metal–ligand-n forms as the following steps [22]. The equilibrium constants, K1, K2, K3, … Kn are called stepwise stability constants. The formation of the complex metal-ligandn may also be expressed by the following steps and equilibrium constants.
Where:
M = central metal cation
L = monodentate ligand
N = maximum coordination number for the metal ion M for the ligand
If a complex ion is slow to reach equilibrium, it is often possible to apply the method of isotopic dilution to determine the equilibrium concentration of one or more of the species. Most often radioactive isotopes are used.
This method was extensively used by Werner and others to study metal complexes. In the case of a series of complexes of Co(III) and Pt(IV), Werner assigned the correct formulae on the basis of their molar conductance values measured in freshly prepared dilute solutions. In some cases, the conductance of the solution increased with time due to a chemical change, e.g.,
It is concluded that the information presented is very important to determine the stability constant of the ligand metal complexes. Some methods like spectrophotometric method, Bjerrum’s method, distribution method, ion exchange method, electrometric techniques, and potentiometric method have a huge contribution in quantitative analysis by easily finding the stability constants of metal complexes in aqueous solutions.
All the authors thank the Library of University of Delhi for reference books, journals, etc. which helped us a lot in reviewing the chapter.
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\\n"}]'},components:[{type:"htmlEditorComponent",content:"In each instance of a possible Conflict of Interest, IntechOpen aims to disclose the situation in as transparent a way as possible in order to allow readers to judge whether a particular potential Conflict of Interest has influenced the Work of any individual Author, Editor, or Reviewer. IntechOpen takes all possible Conflicts of Interest into account during the review process and ensures maximum transparency in implementing its policies.
\n\nA Conflict of Interest is a situation in which a person's professional judgment may be influenced by a range of factors, including financial gain, material interest, or some other personal or professional interest. For IntechOpen as a publisher, it is essential that all possible Conflicts of Interest are avoided. Each contributor, whether an Author, Editor, or Reviewer, who suspects they may have a Conflict of Interest, is obliged to declare that concern in order to make the publisher and the readership aware of any potential influence on the work being undertaken.
\n\nA Conflict of Interest can be identified at different phases of the publishing process.
\n\nIntechOpen requires:
\n\nCONFLICT OF INTEREST - AUTHOR
\n\nAll Authors are obliged to declare every existing or potential Conflict of Interest, including financial or personal factors, as well as any relationship which could influence their scientific work. Authors must declare Conflicts of Interest at the time of manuscript submission, although they may exceptionally do so at any point during manuscript review. For jointly prepared manuscripts, the corresponding Author is obliged to declare potential Conflicts of Interest of any other Authors who have contributed to the manuscript.
\n\nCONFLICT OF INTEREST – ACADEMIC EDITOR
\n\nEditors can also have Conflicts of Interest. Editors are expected to maintain the highest standards of conduct, which are outlined in our Best Practice Guidelines (templates for Best Practice Guidelines). Among other obligations, it is essential that Editors make transparent declarations of any possible Conflicts of Interest that they might have.
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