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",isbn:"978-1-83962-547-3",printIsbn:"978-1-83962-546-6",pdfIsbn:"978-1-83962-548-0",doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!0,hash:"e5ba02fedd7c87f0ab66414f3b07de0c",bookSignature:" John P. Tiefenbacher",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/10765.jpg",keywords:"Managing Urbanization, Managing Development, Managing Resource Use, Drought Management, Flood Management, Water Quality Monitoring, Air Quality Monitoring, Ecological Monitoring, Modeling Extreme Natural Events, Ecological Restoration, Restoring Environmental Flows, Environmental Management Perspectives",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:null,numberOfDimensionsCitations:null,numberOfTotalCitations:null,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"January 12th 2021",dateEndSecondStepPublish:"February 9th 2021",dateEndThirdStepPublish:"April 10th 2021",dateEndFourthStepPublish:"June 29th 2021",dateEndFifthStepPublish:"August 28th 2021",remainingDaysToSecondStep:"21 days",secondStepPassed:!1,currentStepOfPublishingProcess:2,editedByType:null,kuFlag:!1,biosketch:"A geospatial scholar working at the interface of natural and human systems, collaborating internationally on innovative studies about hazards and environmental challenges. Dr. Tiefenbacher has published more than 200 papers on a diverse array of topics that examine perception and behaviors with regards to the application of pesticides, releases of toxic chemicals, environments of the U.S.-Mexico borderlands, wildlife hazards, and the geography of wine.",coeditorOneBiosketch:null,coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"73876",title:"Dr.",name:"John P.",middleName:null,surname:"Tiefenbacher",slug:"john-p.-tiefenbacher",fullName:"John P. Tiefenbacher",profilePictureURL:"https://mts.intechopen.com/storage/users/73876/images/system/73876.jfif",biography:"Dr. John P. Tiefenbacher (Ph.D., Rutgers, 1992) is a professor of Geography at Texas State University. His research has focused on various aspects of hazards and environmental management. Dr. Tiefenbacher has published on a diverse array of topics that examine perception and behaviors with regards to the application of pesticides, releases of toxic chemicals, environments of the U.S.-Mexico borderlands, wildlife hazards, and the geography of wine. More recently his work pertains to spatial adaptation to climate change, spatial responses in wine growing regions to climate change, the geographies of viticulture and wine, artificial intelligence and machine learning to predict patterns of natural processes and hazards, historical ethnic enclaves in American cities and regions, and environmental adaptations of 19th century European immigrants to North America's landscapes.",institutionString:"Texas State University",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"1",totalChapterViews:"0",totalEditedBooks:"6",institution:{name:"Texas State University",institutionURL:null,country:{name:"United States of America"}}}],coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"12",title:"Environmental Sciences",slug:"environmental-sciences"}],chapters:null,productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},personalPublishingAssistant:{id:"194667",firstName:"Marijana",lastName:"Francetic",middleName:null,title:"Ms.",imageUrl:"https://mts.intechopen.com/storage/users/194667/images/4752_n.jpg",email:"marijana@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, copyediting 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:"1591",title:"Infrared Spectroscopy",subtitle:"Materials Science, Engineering and Technology",isOpenForSubmission:!1,hash:"99b4b7b71a8caeb693ed762b40b017f4",slug:"infrared-spectroscopy-materials-science-engineering-and-technology",bookSignature:"Theophile Theophanides",coverURL:"https://cdn.intechopen.com/books/images_new/1591.jpg",editedByType:"Edited by",editors:[{id:"37194",title:"Dr.",name:"Theophanides",surname:"Theophile",slug:"theophanides-theophile",fullName:"Theophanides Theophile"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"3092",title:"Anopheles mosquitoes",subtitle:"New insights into malaria vectors",isOpenForSubmission:!1,hash:"c9e622485316d5e296288bf24d2b0d64",slug:"anopheles-mosquitoes-new-insights-into-malaria-vectors",bookSignature:"Sylvie Manguin",coverURL:"https://cdn.intechopen.com/books/images_new/3092.jpg",editedByType:"Edited by",editors:[{id:"50017",title:"Prof.",name:"Sylvie",surname:"Manguin",slug:"sylvie-manguin",fullName:"Sylvie Manguin"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"3161",title:"Frontiers in Guided Wave Optics and Optoelectronics",subtitle:null,isOpenForSubmission:!1,hash:"deb44e9c99f82bbce1083abea743146c",slug:"frontiers-in-guided-wave-optics-and-optoelectronics",bookSignature:"Bishnu Pal",coverURL:"https://cdn.intechopen.com/books/images_new/3161.jpg",editedByType:"Edited by",editors:[{id:"4782",title:"Prof.",name:"Bishnu",surname:"Pal",slug:"bishnu-pal",fullName:"Bishnu Pal"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"72",title:"Ionic Liquids",subtitle:"Theory, Properties, New Approaches",isOpenForSubmission:!1,hash:"d94ffa3cfa10505e3b1d676d46fcd3f5",slug:"ionic-liquids-theory-properties-new-approaches",bookSignature:"Alexander Kokorin",coverURL:"https://cdn.intechopen.com/books/images_new/72.jpg",editedByType:"Edited by",editors:[{id:"19816",title:"Prof.",name:"Alexander",surname:"Kokorin",slug:"alexander-kokorin",fullName:"Alexander Kokorin"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"1373",title:"Ionic Liquids",subtitle:"Applications and Perspectives",isOpenForSubmission:!1,hash:"5e9ae5ae9167cde4b344e499a792c41c",slug:"ionic-liquids-applications-and-perspectives",bookSignature:"Alexander Kokorin",coverURL:"https://cdn.intechopen.com/books/images_new/1373.jpg",editedByType:"Edited by",editors:[{id:"19816",title:"Prof.",name:"Alexander",surname:"Kokorin",slug:"alexander-kokorin",fullName:"Alexander Kokorin"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"57",title:"Physics and Applications of Graphene",subtitle:"Experiments",isOpenForSubmission:!1,hash:"0e6622a71cf4f02f45bfdd5691e1189a",slug:"physics-and-applications-of-graphene-experiments",bookSignature:"Sergey Mikhailov",coverURL:"https://cdn.intechopen.com/books/images_new/57.jpg",editedByType:"Edited by",editors:[{id:"16042",title:"Dr.",name:"Sergey",surname:"Mikhailov",slug:"sergey-mikhailov",fullName:"Sergey Mikhailov"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"371",title:"Abiotic Stress in Plants",subtitle:"Mechanisms and Adaptations",isOpenForSubmission:!1,hash:"588466f487e307619849d72389178a74",slug:"abiotic-stress-in-plants-mechanisms-and-adaptations",bookSignature:"Arun Shanker and B. 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"}},{type:"book",id:"3621",title:"Silver Nanoparticles",subtitle:null,isOpenForSubmission:!1,hash:null,slug:"silver-nanoparticles",bookSignature:"David Pozo Perez",coverURL:"https://cdn.intechopen.com/books/images_new/3621.jpg",editedByType:"Edited by",editors:[{id:"6667",title:"Dr.",name:"David",surname:"Pozo",slug:"david-pozo",fullName:"David Pozo"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}}]},chapter:{item:{type:"chapter",id:"60594",title:"Mitochondrial Trafficking by Prohibitin-Kinesin-Myosin- Cadherin Complex in the Eye",doi:"10.5772/intechopen.75994",slug:"mitochondrial-trafficking-by-prohibitin-kinesin-myosin-cadherin-complex-in-the-eye",body:'\nMitochondria are the highly dynamic cellular organelles that form a dynamic network to regulate calcium balance, energy metabolism, and apoptotic signaling [1, 2, 3, 4, 5, 6, 7, 8]. Mitochondria alter their morphology repeatedly through the collective actions of fission as a separation of a single organelle into multiple autonomous structures, fusion as the combination of multiple structures to form single organelle, as well as movement along cytoskeletal paths [5, 9]. These combined actions occur concurrently in major cell types to regulate the cell fate.
\nTo maintain the balance that regulates overall morphology and cytoskeletal stability many specialized molecules including dynamin family of proteins play critical roles [10, 11]. Growing body of evidence demonstrates that disruptions of mitochondrial network lead to multiple human pathologies, including metabolic, genetic, cardiovascular diseases, as well as neurogenerative diseases and cancers [12, 13, 14, 15]. Several studies provided the evidence that mitochondria play a critical role in the progression of age-related diseases, including age-related macular degeneration (AMD) [16, 17, 18, 19, 20, 21]. The damage of mitochondrial DNA could be the key factor involved in altered vascular endothelial growth factor (VEGF) secretion, retinal pigment epithelium (RPE) dysfunction, and cell death during the progression of AMD [22, 23].
\nThe current study aimed to examine the correlation between alterations in mitochondrial morphology and mitochondrial dysfunction. For quantitative analysis of mitochondrial morphology, we introduced the mitochondrial index that includes network size, mitochondrial content and surface area. Mitochondrial interconnectivity and elongation were determined systematically using a computational model in three dimensions, showing a mitochondrial- endoplasmic reticulum (ER)-nuclear hole as open space for trafficking at the beginning of apoptosis under oxidative stress.
\nThe assessment of average circularity showed mitochondrial elongation which is sensitive to fragmented vs. normal shaped mitochondria. The average area/perimeter ratio showed normal or stressed mitochondria as a highly interconnected mass of reticular network. Previously, we observed that prohibitin translocalizes between the nucleus and mitochondria under oxidative stress conditions to influence mitochondrial dynamics [24]. We observed anterograde signaling from the nucleus to mitochondria using a prohibitin shuttle under stress in the retina, as well as the retrograde shuttling of prohibitin from mitochondria to the nucleus in the RPE. In addition, cytoskeletal reorganization, tubulin/vimentin depolymerization and increased phosphorylations were observed in stressed mitochondria [25, 26, 27].
\nIn this study, mitochondrial dynamics was further analyzed in mitochondrial trafficking complex using prohibitin immunoprecipitation. We found a motor-based protein complex that includes kinesin 19 (93 kDa), myosin 9 (110 kDa), and cadherin isoforms (88 kDa) to regulate the mitochondrial-nuclear communication. Finally, we have established a comprehensive mitochondrial interactome map by combining several independent sets of interaction data. Our interactome map provides an integrated information on the hidden apoptotic pathway, cytoskeletal rearrangement, nitric oxide signaling, ubiquitination, and mitochondrial network in neurodegeneration.
\nRetinal pigment epithelial cells (ARPE-19) were purchased from ATCC (Manassas, VA) and cultured in Dulbecco’s modified Eagle’s medium (DMEM) supplemented with fetal bovine serum (FBS; 10%) and penicillin/streptomycin (1%) at 37°C in a humidified atmosphere of 5% CO2 in air as suggested by the manufacturer. Cells were used between passages 8–9.
\nRetinal progenitor cells (HRP) were kindly donated by Dr. Harold J. Sheeldo (University of North Texas Health Science Center) and were cultured at the same condition as ARPE-19 cells.
\nPrior to all experiments, confluent ARPE-19 cells were incubated with fresh medium for 12 h and washed with phosphate buffered saline (PBS) three times. ARPE-19 cells were incubated with an oxidant, tert-butyl hydroperoxide (t-BuOOH, 200 μM, Sigma-Aldrich, St.Louis, MO), in serum-free medium for 0.5, 1, 2, 4, 6, 8, 12, and 24 h and representative images were presented. After the treatment, medium was removed, cells were washed with PBS and harvested for future analysis. Cells were lysed for experiments, including, immunoprecipitation, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS−PAGE), Western blot analysis, immunocytochemistry, and mass spectrometry analysis.
\nTo compare with other stress environment, ARPE-19 cells were incubated under intense light (210 μmoles/m2/s photon flux; 7000 lx) for 1 h in serum-free media and analyzed by SDS-PAGE/Western blotting, or immunocytochemistry.
\nLipids were extracted from ARPE-19 cells using cholorform/methanol (2:1, v/v) and organic solvent was evaporated under a gentle nitrogen stream and dissolved in chloroform for analysis by HPLC and mass spectrometry.
\nAll experiments were repeated (N = 3–10 biological samples) with technical duplicate or triplicate. Statistical analysis was performed using StatView software and statistical significance was determined by variance (ANOVA) or unpaired Student’s t test when appropriate.
\nHuman postmortem donor eye tissues were used following the tenets of the Declaration of Helsinki. Human AMD retinas (8 mm macular and peripheral punches), RPE (8 mm central and peripheral punches), and age-matched control eyes (N = 9, biological triplicate x technical triplicate) were provided by the Lions Eye Bank (Moran Eye Center, University of Utah). Phosphoproteome of macular (I), peripheral retina (II), central RPE (III), and peripheral RPE (IV) was compared to age-matched control donor eyes to determine region-specific senescence-associated molecular mechanisms during AMD progression. Phosphoproteins were enriched by charge-based spin column chromatography and resolved by 2D gel electrophoresis as previously reported [28]. In addition, trypsin digested phosphopeptides from whole lysates were enriched using Ga3+/TiO2 immobilized metal ion chromatography. Eluted phosphopeptides were analyzed using mass spectrometry including MALDI-TOF-TOF and ESI MS/MS.
\nTo analyze mitochondrial morphology, Cells were incubated with 100 nM MitoTracker Orange (Molecular Probes). Cells were fixed using 10% formaldehyde (25 min) and the membrane was permeabilized using 0.2% Triton X-100 (20 min), followed by blocking (0.05% Tween 20, 10% FBS, 1 h) and incubation overnight at 4°C with anti-prohibitin antibody (1:500; Genemed Synthesis, San Antonio). Prohibitin was visualized using Alexa Fluor 488-secondary IgG antibody (1:700; 1 h at 25°C; Molecular Probes). The nuclei were visualized by incubation with DAPI (4, 6-diamidino-2-phenylindole) added to VECTASHIELD Mounting Medium (Vector Laboratories, Burlingame, CA). A fluorescence microscopy was used for image analysis (Zeiss AxioVert 200 M Apo Tome, 63×).
\nARPE-19 cells were rinsed (Modified Dulbecco’s PBS) and lysed using immunoprecipitation (IP) lysis buffer (pH 7.4) containing Tris (25 mM), NaCl (150 mM), EDTA (1 mM), NP-40 (1%), glycerol glycerol (5%), and protease inhibitor cocktail by incubating on ice for 5 min with periodic sonication (3 × 5 min), followed by centrifugation (13,000 × g, 10 min). Proteins (1 mg/mL, 200–400 μL) were loaded for immunoprecipitation and nonspecific bindings were avoided using control agarose resin cross-linked by 4% bead agarose. Amino-linked protein-A beads were used to immobilize anti-prohibitin antibody with a coupling buffer (1 mM sodium phosphate, 150 mM NaCl, pH 7.2), followed by incubation (room temperature, 2 h) with sodium cyanoborohydride (3 μL, 5 M). Columns were washed using a washing buffer (1 M NaCl), and protein lysate was incubated in the protein A-antibody column with gentle rocking overnight at 4°C. The unbound proteins were spun down as flow-through, and the column was washed three times using the washing buffer (1 M NaCl) to remove nonspecific binding proteins. The prohibitin-interacting proteins were eluted by incubating with elution buffer for 5 min at room temperature. The eluted proteins were equilibrated with Laemmli sample buffer (5X, 5% β-mercaptoethanol). Eluted proteins were separated using SDS–PAGE and visualized using Coomassie blue (Pierce, IL) or silver staining kit (Bio-Rad, Hercules, CA). Prohibitin and p53 were visualized using Western blot analysis. Proteins were identified by mass spectrometry analysis.
\nProtein bands were excised into 1 × 1 × 1 mm cubes. The Coomassie-stained or silver-stained gel pieces were incubated using a Coomassie destaining buffer (200 μL of 50% MeCN in 25 mM NH4HCO3, pH 8.0, room temperature, 20 min) or silver destaining buffer (50% of 30 mM potassium ferricyanide, 50% of 100 mM sodium thiosulfate, 5–10 min). The gel pieces were dehydrated (200 μL, MeCN) and vacuum-dried (Speed Vac, Savant, Holbrook, NY). Proteins were reduced (10 mM DTT, 100 mM NH4HCO3, 30 min, 56°C) and were alkylated (55 mM iodoacetamide, 100 mM NH4HCO3, 20 min, room temperature in the dark). Proteins were digested using trypsin (13 ng/μL sequencing-grade from Promega, 37°C, overnight) in NH4HCO3 (10 mM) containing MeCN (10%). The peptides were enriched using a buffer (50 μL, 50% MeCN in NH4HCO3, 5% formic acid, 20 min, 37°C). Dried peptides were dissolved in the mass spectrometry sample buffer (5–10 μL, 75% MeCN in NH4HCO3,1% trifluoroacetic acid). Alpha-cyano-4-hydroxycinnamic acid (5 mg/mL, Sigma-Aldrich, St. Louis, MO) was freshly dissolved in a matrix buffer (50% MeCN, 50% NH4HCO3, 1% triflouroacetic acid) and centrifuged (13,000× g, 5 min). The peptide-matrix mixtures (0.5 μL) were spotted onto the MALDI target plate (Ground steel, Bruker Daltonics, Germany). Mass spectrometer and all spectra were calibrated using a known peptide, including trypsin (842.5099, 2211.105 Da). The mass spectrum was recorded in 800–3000 Da range using Flex MALDI-TOF mass spectrometer (Bruker Daltonics, Germany, 70–75% laser intensity, 100–300 shots). Mass spectrometry data were analyzed using Flex analysis software (Bruker Dal- tonics, Germany). Peptides were identified using the Mascot software (Matrix Science) and NCBI/SwissProt database (zero mismatch cleavage, carbamidomethyl cysteine, methionine oxidation, 50–300 ppm mass tolerance). Peptide identification was evaluated based on Mascot MOWSE score, number of matched peptides, and protein sequence coverage. MOWSE score is expressed as -10logP as a probability value to compute the composite probability P.
\nThe connectivity, the number of mitochondrial branch points, and the interactive 3D visualization of isosurfaces were examined to identify the contact area between mitochondria and other organelles.
\nMitochondria were stained using MitoTracker Orange/Red or rhodamine 123. Mitochondrial interconnectivity and elongation were analyzed systematically using computational software, including Mito-Morphology macro, Mitograph 2.0, Imaris 8.2.1., and SOAX 3.6.1.
\nMitochondrial size and morphology were analyzed using the software connected to Image J software (Ruben Dagda:
Mitochondrial shape, including fused, fragmented, tubular, swollen, branched, uniform, and perinuclear clustering, was examined quantitatively. Mitochondrial filaments in three dimensions and mitochondrial parameters in ARPE-19 cells were calculated mathematically using Image J and Imaris (v8.2.1) software. The connectivity, the number of mitochondrial branch points, and the interactive 3D visualization of isosurfaces were examined to identify the contact between mitochondria and other organelles.
\nMitochondrial signaling in a network-based interactome map between genome, proteome, and metabolome of AMD was established using proteome data and bioinformatics software. The protein-protein interaction was established using the Münich Information Center for Protein Sequence (MIPS), Biomolecular Interaction Network Database (BIND), the Database of Interacting Proteins (DIP), the Molecular Interaction Database (MINT), the Protein Interaction Database (IntAct), and STRING.
\nInteraction mapping of prohibitin was determined using immunoprecipitation, followed by mass spectrometry analysis. Prohibitin binding proteins in the RPE were connected using STRING 10.0 software (
Prohibitin interactions were confirmed using eight sources that include neighborhood, gene fusion, co-occurence, high-throughput interaction experiments, databases, homology, conserved co-expression, and published knowledge, including ExPASy (
AMD and oxidative biomarkers interactome were established using protein–protein interaction map software and databases, including STRING 10.0 (
The genome regulatory network was connected to the proteome network using Uniprobe and JASPAR. Protein phosphorylations were examined by phosphoprotein/peptide enrichment, followed by mass spectrometry analysis. Phosphorylations were compared to Phospho.ELM, and PhosphoSite. The metabolome mapping was established using KEGG and BIGG databases.
\nTo understand how mitochondria regulate their morphology and function, we first analyzed mitochondrial morphology quantitatively in ARPE-19 cells subjected to oxidative stress conditions using a systematic computational model (Figure 1). Representative mitochondrial images at selected time points (0.5, 1, 8, 24 h) are shown for clear comparison Figure 1). We examined mitochondrial area, circularity, perimeter, content as well as cellular area to identify changes between healthy and injured mitochondria. Previously, our in vitro data using RPE cells demonstrated the positive correlation between apoptotic signaling and mitochondria-nucleus prohibitin shuttling. Our previous studies suggest that cellular distribution and the total volume of mitochondria could be affected by microtubules, intermediate filaments and cardiolipin [24, 25, 26, 27, 29, 30].
\nQuantitative analysis of mitochondrial morphology: representative images of MitoTracker Orange-labeled mitochondria from ARPE-19 cells exposed to t-BuOOH for 0.5–24 h or light for 1 h are shown here. A. ARPE-19 cells under oxidative stress were analyzed by immunocytochemistry using MitoTracker. B. Mitochondrial content was represented by 2D graph (radius/intensity) showing decreased size and fragmentation pattern under stress conditions. C. Mitochondria in ARPE-19 cells were presented in 3D structure using Image J software.
Our results showed that the connectivity, the number of mitochondrial branch points, and the interactive isosurfaces were altered at the contact sites between mitochondria and other organelles. Under extended oxidative stress (1, 8, 24 h) and intense light (7000 lx, 1 h), we observed a decrease in mitochondrial size, presence of fragmented filaments (red arrows), and holes on the organelle contact sites. Under intense light condition, mitochondria in ARPE-19 cells were decreased and fragmented as shown in oxidative stress (1–8 h).
\nNext, mitochondrial perimeter vs. circularity was examined to determine the correlation between mitochondrial morphology and oxidative stress (Figure 2). We hypothesized that some mitochondrial indexes that include circularity and perimeter ratio may represent mitochondrial dynamics. We calculated mitochondrial area, perimeter, minor axis, and circularity to conclude that specific mitochondrial ratio correlated positively with stress kinetics.
\nQuantitative analysis of mitochondrial morphology: perimeter vs. circularity. X axis represents time of ARPE-19 cells under oxidative stress and Y axis represents mitochondrial index on perimeter vs. circularity ratio in arbitrary units. Selected time points are 0, 8, 24 h were shown for clarity [24]. Our calculation demonstrated that mitochondria under oxidative stress change their morphology to circular shape for fusion, followed by fragmentation toward greater degree of roundness and circularity. Total area of mitochondria decreased to 40–50% and both perimeter/circular mitochondria were downregulated to 60–70%. Area/perimeter normalized to circularity ratio of mitochondria was decreased to 63% (1 h oxidative stress), showing a positive correlation between mitochondrial morphology changes and apoptotic RPE.
The average mitochondrial area/perimeter ratio normalized to the minor axis suggests that specific conditions may induce mitochondrial swelling (Figure 3). Time-dependent decrease of minor axis and mitochondrial area/perimeter normalized to the circularity was noticed under stress condition. Our previous proteomic study demonstrated that tubulin/vimentin depolymerization and phosphorylations increased in stressed mitochondria [25].
\nMitochondrial index: mitochondrial area/perimeter/minor axis vs. minor axis vs. area/perimeter/circularity. X axis represents stressed time (hrs) of ARPE-19 under oxidants and Y axis represents mitochondrial index showing mitochondrial area/perimeter/minor axis (red), compared to mitochondrial minor axis (black), and mitochondrial area/perimeter/mitochondrial circularity (blue) in arbitrary units.
To understand mitochondrial dynamics in detail, mitochondrial trafficking complex was examined. Subcellular fractionation, immunoprecipitation using primary prohibitin antibody, native gel, and mass spectrometry analysis suggest that motor protein complex may determine mitochondrial dynamics and retrograde signaling under stress conditions. Molecular motor complex contains plus-end-directed kinesin 19, myosin 9, protocadherin gA7, and prohibitin (Figure 4). The molecular motor/adaptor/receptor complex mediates mitochondrial dynamics. Motor proteins, including kinesin and myosin, facilitate mitochondrial trafficking along the cytoskeleton, mainly microtubules, actin polymers and intermediate filaments (Figure 5). Domain analysis of mitochondrial trafficking complex showed that plus-end-directed kinesin 19 (ATP and Mg2+ binding domains), myosin 9 (myosin head motor domain, SH3 domain, ATP binding domain), protocadherin gA7 (cadherin repeat and Ca2+ binding domain), and prohibitin (PX domain, lipid binding pocket) exist in the trafficking complex.
\nMitochondrial Trafficking Complex in vitro: Retrograde vs. Anterograde Signal. Protein complex in ARPE-19 (RPE) and HRP (retina) cells were analyzed using immunoprecipitation and mass spectrometry. Under normal condition, trafficking complex including prohibitin translocalizes into mitochondria (anterograde) whereas trafficking complex moves into the nucleus (retrograde) under oxidative stress in RPE cells. The molecular motor/adaptor/receptor complex mediates mitochondrial anterograde vs. retrograde signaling. However, in the retina, retrograde signal (mitochondria to the nucleus) is dominant under normal condition, probably due to increased p53 signaling (prohibitin found in the nucleus).
Domain analysis of mitochondrial trafficking complex: ATP, Ca2+, and lipid-dependent signaling. Prohibitin binding proteins were analyzed using bioinformatics software and databases, including iHOP, InterPro (https://www.ebi.ac.uk/interpro/), Expasy/Prosite (https://prosite.expasy.org/), conserved domain search (https://www.ncbi.nlm.nih.gov/Structure/cdd/wrpsb.cgi), Motif (https://molbiol-tools.ca/Motifs.htm) and Pfam (http://pfam.xfam.org/). Kinesin 19 contains ATP binding domain and kinesin motor domain, whereas Myosin 9 has SH3, ATP binding, TATA binding, and myosin motor domains. Protocadherin γA7 includes repeat domain and calcium binding sequences. Prohibitin contains PX domain and the second lipid binding domain.
In order to correlate our in vitro findings with human pathology, we analyzed mitochondrial trafficking complex in human postmortem AMD eyes using a proteomic approach (Figure 6). RPE and retina tissues (central vs. peripheral) from AMD eyes and age-matching control eyes were analyzed by phosphoproteomics and mass spectrometry analysis. We observed different expression levels of prohibitin, inositol receptor, calponin, ankyrin, guanylate cyclase, and NADP ubiquinone oxidoreductase in the RPE and pyruvate kinase, PP2A, creatine kinase, PAK S/T kinase, vimentin, FES tyrosine kinase and dynamin like protein in the retina from AMD samples compared to control. Our results suggest that mitochondrial trafficking could be a significant determinant of RPE apoptosis by decreased prohibitin. Further, Ca2+, Fe2+, inositide, phosphorylation, and energy imbalance may lead to the accelerated pathogenesis toward AMD.
\nMitochondrial signaling in the retina and RPE in vivo using human AMD eyes: mitochondrial trafficking is a significant determinant of RPE apoptosis. RPE and retina tissues (central vs. peripheral) from AMD eyes and age-matching control eyes were analyzed using phosphoproteomics and mass spectrometry analysis. We observed different expressions of inositol receptor, calponin, ankyrin, guanylate cyclase, and NADP ubiquinone oxidoreductase in the RPE and pyruvate kinase, PP2A, creatine kinase, PAK S/T kinase, vimentin, FES tyrosine kinase and dynamin like protein in the retina from AMD samples compared to control. Altered concentrations of mitochondrial complex, phosphoproteins, and ATP/ADP may lead to premature senescence in RPE cells.
It is proposed that specific organelles, including mitochondria, melanosome, and phagosome, may use different kinesin and myosin motors for their distribution and trafficking in the RPE [25, 31, 32, 33]. Mitochondrial trafficking could be determined by ATP, Ca2+, and lipid interactions based on their domain analysis [29, 34, 35, 36, 37, 38] and mitochondrial trafficking is a significant determinant of RPE apoptosis [24, 37]. Altered concentrations of mitochondrial complex, phosphoproteins, and ATP/ADP may lead to premature senescence in RPE cells [27]. Our enriched phosphoproteins and phosphopeptides analysis demonstrated that altered inositol triphosphate receptor, ankyrin, NADP reactions exist in AMD (Figure 6). Regulation of mitochondrial complex/lipid ratio and the energy producing machinery may enable enhanced longevity of RPE cells.
\nNext, a 3D surface model was used to analyze mitochondrial nodes, edges, branches, and tubular filaments (Figure 7). Cellular distribution and the total volume were affected by microtubules, intermediate filaments and cardiolipin. A 3D model showed that mitochondrial contact sites with endoplasmic reticulum (ER) and/or the nucleus were opened irreversibly under extended stress (24 h).
\nA 3D surface model and a graph representation by nodes, edges, branches, and tubular filaments: Mitochondrial filaments in three dimensions in RPE cells were calculated quantitatively. The connectivity, the number of mitochondrial branch points, and the interactive 3D visualization of isosurfaces were examined to identify the contact point between mitochondria and other organelles, including ER and the nucleus (white arrow). Mitochondria under oxidative stress (24 hrs) decreased their average perimeter (49%), average area (28%), area/perimeter (56%), and minor axis (32%).
In order to understand AMD protein network, the new AMD interactome with oxidative biomarkers was established using phosphoproteomics data and a computational model. The current AMD interactome demonstrated that several earlier unrelated to AMD proteins, including ubiquitin, peroxiredoxin, MAP kinase, BUB 1/3, vimentin and crystalline could be involved in AMD progression, suggesting that cytoskeletal protein phosphorylation, crystalline aggregation, and mitochondrial signaling may contribute to RPE apoptosis (Figure 8). To confirm oxidative stress biomarkers, specific cytoskeletal protein changes were determined in vivo using animal model previously (C3H female mice, 7 weeks old) [25, 30, 38]. Neurofilament, vimentin, and tubulin were upregulated under 24 h constant light compared to 12 h dark/12 h light condition [38].
\nGenome-proteome-metabolome mapping in AMD: retrograde mitochondrial signaling. The protein interactome was established using STRING software and our proteomics data. The genome regulatory network was connected to the proteome network using Uniprobe and JASPAR. Protein phosphorylations were examined by phosphoprotein/peptide enrichment, followed by mass spectrometry analysis. Phosphorylations were compared to Phospho.ELM, and PhosphoSite. The metabolome mapping was established using KEGG and BIGG databases. Based on our proteomics and the interactome data that identified altered signaling of apoptosis in the retina and RPE both in vitro and in vivo, the pathological pathway determined by the AMD interactome could yield suitable targets for anti-apoptotic and anti-angiogenic therapy: (1) mitochondrial dysfunction in the peripheral RPE (prohibitin, ATP synthase); (2) oxidative stress including intense and constant light (peroxiredoxin, thioredoxin, glutathione S-transferase); (3) cytoskeletal remodeling by microtubule, actin filament, and intermediate filament (vimentin, actin, tubulin); (4) high concentration of nitric oxide (nitric oxide synthase), (5) hypoxia (HIF1, erythropoietin, VEGF); (6) disrupted circadian clock (melatonin); (7) apoptotic downstream (pJAK2, pSTAT3, Bclxl, caspases); (8) altered lipid concentrations (cardiolipin, cholesterol); (9) altered visual cycle (CRABP, CRALBP, RPE65); (10) altered energy metabolism (S/T vs. Y kinases, carnitine, pyruvate, ATP synthase); (11) aggregation of heat shock proteins and crystallins; and (12) inflammation (CFH, C3, collagen, vitronectin).
The current study determined the mitochondrial morphology quantitatively using a mathematic model and mitochondrial trafficking complex under stress conditions. Our data suggest that the kinesin-myosin-cadherin-prohibitin complex could be involved in anterograde mitochondrial trafficking, whereas PKUb S/T kinase-myosin-PI3K-lamin B2 bindings may regulate an energy demanding retrograde transport of mitochondria [25, 39, 40, 41, 42, 43]. Prohibitin binding with a trafficking protein complex may regulate the bidirectional transport of mitochondria along actin microfilaments, intermediate filaments, and microtubules. The mitochondrial trafficking complex implies that a specific mechanism of communication may exist in the ATP and Ca2+ demanding regions. Mitochondrial dysfunction, altered dynamics, impaired transport, and turnover perturbation are associated with AMD.
\nOxidative stress-induced apoptosis is the final cell death pathway in many irreversible ocular diseases that include AMD. While the end point of apoptosis is well established, the knowledge of early biochemical reactions and specific molecular players has been elusive. We have examined early biosignatures and mechanisms of retinal and RPE cell death under oxidative stress [44]. Our previous studies demonstrated that not only intense light but also constant moderate light and mild oxidative stress may trigger induction of anti-apoptotic Bcl-xL and erythropoietin (EPO) as well as pro-apoptotic caspases [24, 25, 27, 28, 29, 37, 38, 45, 46, 47]. We determined that protein modifications, including nitration and phosphorylation, were altered under oxidative stress possibly due to excess of NO production [26, 48, 49, 50].
\nThe analysis of AMD interactome using proteome-genome-metabolome network suggests that there is a positive correlation between mitochondrial retrograde signaling and AMD progression. The AMD interactome suggests: (1) network-based interactions among AMD-related hub proteins that include UBC, MMP2, BCL, PRDX, ATP5O, C3, TF, and CRYAB, (2) increased local interactions between oxidative stress, complement activation, transcription, metabolism, (3) AMD module as a cluster in the same network neighborhood, (4) potential causal molecules including Ca2+, Fe2+, ATP/ADP, OPO42−, lipids, (5) altered cytoskeleton, microtubule, abnormal mitochondrial signaling.
\nThe mitochondrial interactome provides a base for better understanding of oxidative stress-induced apoptosis and the mechanism of age-related diseases, including AMD. As a consequence, an effective treatment of neurodegenerative diseases based on the modulation of mitochondrial network is expected to result.
\nEntangled photon pairs are one of the key elements for research and in emerging quantum applications with successful results in quantum foundations [1, 2], quantum communication [3, 4, 5], and quantum information [6, 7, 8]. Thus far, nonlinear crystals exhibiting spontaneous parametric down-conversion (SPDC) [9, 10, 11] have been the main source of generating entangled photon pairs for use in these areas. This type of source results in photon pairs that exhibit near-unity entanglement fidelity, high degrees of single-photon purity and indistinguishability in each emission mode, and high temporal correlation. Moreover, these sources perform at or near room temperature. However, there are fundamental limitations to such sources, which limit their performance and scalability for use in quantum photonics; an ideal source is imperative for optimal performance. One key feature of an ideal source of entangled photons is the ability to perform on-demand, i.e., source triggering and extraction of light must be possible with near-unity efficiency. SPDC sources follow a stochastic process and therefore generate entangled photon pairs at random. Moreover, the probability of multiphoton generation follows a Poisson distribution, and thus entanglement fidelity, single-photon purity, and photon indistinguishability [12] degrade when the pump power is increased [13]. As a result, these sources only operate at extremely low pair-production efficiencies,
Semiconductor quantum dots [15] are capable of generating pairs of entangled photons based on a process called the biexciton (XX)-exciton (X) cascade [16]; this cascade process is shown in Figure 1. The
The XX-X cascade. In the XX state, holes with jz=±32 and electrons with jz=±12 are paired, resulting in exciton states with jz=±1. The two e-h pairs will then lead to two different recombination pathways, with the final state being a superposition of these two paths, i.e., Ψ=12RL+LR. For a more detailed description of the QDs’ electronic structure, please refer to ref. [17].
Over the past three decades, QDs have been extensively studied with recent advancements, as compared to other solid state quantum emitters [18, 19, 20, 21], and have produced sources which exhibit features closest to an ideal photon source [22]. The first generation of QDs was self-assembled [23, 24, 25], which resulted in QDs with various sizes and imperfect symmetry due to the random nature of the formation process [13]. Moreover, since the bulk semiconductor material possessed a high refractive index, these self-assembled QDs typically suffered from isotropic emission and total internal reflection at the semiconductor-air interface and thus exhibited a low light-extraction efficiency of
Recent developments in micro- and nanoscale crystal growth and fabrication have resulted in structures which have improved the performance of QDs considerably. Enhancement of the spontaneous emission of QDs was first achieved by coupling an ensemble of QDs [27], and later a single QD, to a micro-cavity [28]. More recently, the coupling of QDs to micro-pillar cavities has achieved light-extraction efficiencies as high as 80% [29]. Also, such structures allow for proper control of the charge noise around the QD and thus the suppression of detrimental dephasing processes from the moving charge carriers. Excitingly, as a result, photons with
However, such performance comes at a price. Due to Coulomb interactions [17],
Another important feature of QDs affecting the measured entanglement is the fine-structure splitting (FSS) of the
XX-X cascade in the presence of FSS. (a) R and L basis will be mixed and a precession between the two pathways will be observed. (b) In the H/V basis, the transition energies will be split by FSS =δ.
where
Due to the random nature of the growth process, self-assembled QDs have long suffered from large base asymmetries, which resulted in FSS values larger than the X emission linewidth. This feature will lead to the introduction of a which-path information in the
To reveal the true potential of QDs, proper excitation schemes are needed in addition to engineering sophisticated photonic structures. Until recently, off-resonant excitation had been widely used to generate entangled and single photons from QDs in photonic structures. This scheme excites charge carriers to energy levels above the bandgap of the host semiconductor, and relaxation of the resulted
Direct population of
Schematics of resonant TPE. A linearly polarized pulse is tuned to a virtual state halfway between X and XX transitions (the dashed blue line); and the XX is coherently populated via a two-photon absorption process.
In this review, we focus on attempts to improve the performance of entangled photon generation in by embedding them in photonic nanowires, as well as the effects of different excitation schemes in the performance of such sources. Additionally, we will also cover the improvements achieved in photon extraction efficiency, reduction of the dephasing processes, suppression of multiphoton emission, and enhancing entanglement fidelity of nanowire QD based entangled photon sources.
Embedding QDs in tapered nanowires was initially developed by using top-down approaches via reactive-ion etching [55, 56]. Such photonic structures allow for coupling of the QD emission to the waveguide’s fundamental mode in a broad range of wavelengths,
A novel bottom-up approach to growing tapered nanowires was used in the work by Reimer et al. [57]. This innovative approach allowed, for the first time, the positioning of a QD on the symmetry axis of the nanowire and at a desired height with a precision of ∼100 nm (Figure 4). In this method, the growth of the nanowire core, InP, is initiated by a gold particle which defines the core of the nanowire and ultimately the size of the QD,
Schematic of the bottom-up nanowire growth process and SEM image of a tapered nanowire (right). The growth process is initiated by a gold particle, which defines the dimensions of the QDf. After the quantum dot is grown the waveguide shell and the tapered tip are fabricated around the QD by controlling the growth parameters. This growth process ensures that the QD is placed on-axis of the tapered nanowire waveguide for efficient light extraction.
In terms of brightness, a value of Measuring multiphoton emission and photon indistinguishability of entangled photon sources. 1. Hanbury Brown and Twiss (HBT) setup In order to quantify the multiphoton emission of a source, the second-order correlation function is measured based on a setup first introduced by Hanbury Brown and Twiss [59] (Figure a). In this method, the light emitted from the source is sent to a beam splitter and then detected by two single-photon detectors D1 and D2. By correlating the intensities recorded by the two detectors in different time bins, one can gain information about the emission pattern of the source. Considering the particle nature of photons, if the source emits one and only one photon in each emission mode upon excitation, there will be no simultaneous detection on the two detectors; in other words, there will not be any correlation at zero time delay:Box 1.
with
2. Hong-Ou-Mandel setup
In addition to single-photon emission, for an ideal entangled photon source, the emitted photons in each mode should exhibit perfect indistinguishability. For measuring this feature, the Hong-Ou-Mandel setup is used. Using a setup similar to that the HBT (Figure b) and considering the wave nature of the photons, a HOM measurement enables one to test the degree of indistinguishability of the successive photons. In this scenario, two successive photons are brought together at the beam splitter for interference. Now, at the beam splitter, four different possibilities exist (Figure c); photon 1 may be reflected and photon 2 transmitted (case 1), photon 1 may transmit and photon 2 be reflected (case 2), both may transmit (case 3), and, lastly, both may be reflected (case 4). With reflection from the two sides of the beam splitter differing in a
Following the method introduced by James et al. [60], the first results in measuring the degree of entanglement in bottom-up grown nanowire QDs were reported in 2014 by Versteegh et al. [61]. In this work, using an above-bandgap excitation scheme, the fidelity of the emitted
Two-photon quantum state tomography setup. The setup consists of two pairs of λ/4–λ/2 wave plate sets, which combined with a pair of polarizors perform the projection measurements. A combination of λ/2 and λ/4 wave plates is used to compensate for the birefringence, if it is present in the nanowire (the image is taken from Jöns et al. [62]).
It is important to note that neither of the above-mentioned works addresses the ultimate entanglement fidelity achievable for nanowire QDs. In addition to the projection measurements, a more in-depth analysis is needed in order to reveal the underlying physical mechanisms such as dephasing due to nuclear spins and charge carriers through spin-flip processes. Moreover, the effect of
In an attempt to shed light on these finer aspects of generation of entangled photons in nanowire QDs, Fognini et al. [45] studied an InAsP QD embedded in an InP photonic nanowire, revealing the effects of dephasing,
QD emission spectra. (a) Emission spectrum by excitation via a green laser. Excitations at two different energy levels, wurtzite InP bandgap at 830 nm and donor/acceptor levels at ≈870 nm, were used for performing entanglement measurements; (b) the emission spectrum for 830 nm excitation exhibiting the exciton (X), biexciton (XX), and negatively charged exciton (X−) lines. (c) Excitation at to 870 nm leads to an appearance of a positively charged exciton (X+) and suppression of X−. The spectra in (b) and (c) were taken at the saturation power of X.
Following a similar setup to the one used by Jöns et al. [62] (Figure 5), Fognini et al. [45] conducted two-photon quantum state tomography on the
Dephasing-free entanglement (a) showing the correlation measurements HH+VV and RL+LR−RR+LL. The former does not show any oscillations as H and V are the eigenstates of the Hamiltonian, whereas the latter reveals the precession of the state between Ψ and Φ, according to Eq. (2). The shaded gray bars indicate instances with the highest concurrence, (A), and instances with the lowest imaginary part in the density matrix (B-D). (b) The concurrence extracted from the correlation measurements at each instant of time, for time windows of Δt=100 ps, along the decay time of the exciton. (c) Result of the correlations obtained from the theoretical model (Eq. (4)) with the gray shaded bars indicating similar instances as for (a). (d) Comparison of the measured values of the concurrence with that of the theoretical model, revealing the dephasing-free nature of the XX−X cascade.
Despite the fact that the value for concurrence does not reach near unity and that after a peak around
Starting with the state described by Eq. (2), the expected values for 36 possible projection correlations,
where
To construct the density matrix of the two-photon quantum state, Eq. (4) gives the correlations in all 36 bases with the effect of the detectors’ timing resolution function included. However, two additional factors should be included,
where
Figure 7c shows the calculated
In stark contrast, under non-resonant excitation at the wurtzite InP bandgap, conducting two-photon quantum state tomography reveals the detrimental effect of the surrounding charge noise on the entangled state. By comparing Figure 8a and b, it becomes clear that shortly after the excitation laser moves to the InP bandgap, the detrimental effects of the excessive charge carriers become evident,
Effect of the excitation scheme and detection system. (a) Comparison of the theoretical model and results from quasi-resonant excitation indicate suppression of dephasing during the X decay time. (b) Off-resonant excitation at the wurtzite InP bandgap, leads to the mobility of charge carriers and dephasing of the two-photon quantum state shortly after the XX’s emission. (c) A combination of two different excitation schemes and detection systems were used to produce the four curves: quasi-resonant excitation and avalanche photodiodes (APDs) (red), resonant TPE and APDs (yellow), quasi-resonant excitation and superconducting nanowire single-photon detectors (SNSPDs) (blue), and resonant TPE and SNSPDs (cyan). Imperfect gXX20 values in the case of quasi-resonant excitation (red and blue curves), as well as low timing resolution and relatively high noise level of APDs (red and yellow curves), result in the deterioration of the measured concurrence. Impressively, with the application of resonant TPE, and SNSPDs with a timing resolution of τd∼30ps, and noise level of ∼1Hz, the detection of perfect entanglement is expected.
As mentioned earlier, the drop observed in the measured concurrence is the result of the low timing resolution of the detectors. Therefore, it is expected that once the detection system is improved, an enhancement in the measured concurrence will be observed. Figure 8c shows the result of a simulation when the features of the detection system and/or the excitation scheme have changed. The red curve shows the actual system at hand, quasi-resonant excitation, with
The way in which the curve of concurrence vs. time is affected by the detectors’ response function
where
In the alternate approach, the uncertainty in timing of the arrival of the photons can be interpreted as an uncertainty in measuring the energy of
Detectors’ timing resolution and energy uncertainty. The detectors’ timing resolution, τd, directly leads to an uncertainty in the energy of photons, ΔEτd∼ℏ/2. For the case of a fast detector, τd≪ℏ/δ, this uncertainty can smear out the energy difference between the two decay paths and hence retrieve the entanglement, whereas a slow detector, τd≫ℏ/δ, will push the correlations more toward classical correlations.
In an attempt to realize on-demand entanglement, we have performed performed resonant two-photon excitation on the same sample used by Fognini et al. [45]. The spectrum of the source under resonant TPE is given in Figure 10a. As it is evident from comparing this spectrum with the spectra under non-resonant excitation shown in Figure 6, the abundance of charge carriers surrounding the QD is significantly suppressed, leading to a lower intensity of the
Resonant two-photon excitation of a nanowire QD. (a) The spectrum of the QD under resonant TPE. The X and XX PL transition rates become more similar as compared to non-resonant excitation, indicating an enhanced pair-production efficiency; and the charged exciton is significantly suppressed, indicating a reduction of excessive charged carriers around the QD. (b) The power-dependent XX count rate exhibits a qualitatively similar Rabi oscillation as the regular direct resonant excitations, qualitatively. (c) and (d) show the comparison between results of g20 measurements in the case of quasi-resonant and resonant TPE schemes, for X and XX, respectively. Implementation of resonant TPE significantly reduces the emission time jitter of the two states, as well as multiphoton emission of the XX state.
Moreover, under resonant TPE, the multiphoton emission is significantly suppressed. Figure 10c and d show the results of the second-order correlation function performed on the QD once excited at the donor/acceptor levels and under resonant TPE. For resonant TPE,
The impressive potential for nanowire QDs in detecting entangled photon pairs with near-unity entanglement fidelity is illuminated by the results of the resonant two-photon excitation. Notably, we are now at a point where we can make a comparison between SPDC sources and state-of-the-art QDs in different structures, i.e., self-assembled, micropillar cavities, nanowires, etc. As mentioned earlier, the Poissonian nature of photon-pair emission in SPDC sources limits the performance of such sources to extremely low pair-extraction efficiencies. On the other hand, recent advances in QD growth in various photonic structures have resulted in achieving high entanglement fidelity and high pair-extraction efficiencies, simultaneously. Hüber et al. [67] have reported on measuring an entanglement fidelity of
The result of such a comparison is shown in Figure 11. The blue circles show different values reported for entanglement fidelity vs. pair-extraction efficiency for SPDC sources. The values are taken from [69] and [14]. The dashed line shows the theoretical limit of such sources, following a Poisson distribution for the probability of multiphoton emission [70]. The two solid red squares indicate the result of two measurements performed on nanowire QDs by Jöns et al. [62] and Fognini et al. [45]. The latter work shows both an improvement in the measured entanglement fidelity and an improvement in pair-extraction efficiency. Based on the results shown by Fognini et al. [45] and the improvements gained by performing resonant TPE, we can predict measuring near-unity entanglement fidelity once two important modifications are implemented: the resonant TPE scheme is employed, and the detection system is improved to a fast and low-noise one. The final result that we predict by implementing these two changes is shown by the hollow red square. This is an extrapolation of results reported thus far on nanowire QDs based on the enhancement achieved in pair-extraction efficiency and entanglement fidelity, as well as the analysis presented in Figure 8c. Therefore, it is confidently predicted that nanowire QDs have the potential to surpass and outperform that of SPDC sources, revealing the significant potential of these sources for quantum communication purposes.
Performance of state-of-the-art entangled photon sources. Comparison between various quantum light sources in terms of entanglement fidelity and pair-extraction efficiency. Blue circles represent SPDC sources, values taken from [69] and [14]. The dashed line shows the ultimate theoretical limit of such sources, with multiphoton emission probability following a Poisson distribution. The red triangle shows results for a bare self-assembled QD, whereas the red diamonds show the results for QDs in different photonic structures. The red solid squares indicate the values reported for nanowire QDs so far. The analysis performed by Fognini et al. [45] and the results obtained by Ahmadi et al. [66] strongly suggest that the sources used for these two studies have the capacity to surpass the performance of SPDC sources once excited via resonant TPE and measured with a fast, low-noise detector. The graph is adapted and modified from [62].
In this chapter, we have given a historical overview of previous methods for attaining pairs of entangled photons from a QD, as well as included the latest research and subsequent recent advances toward enhancement of the performance from such sources. Thus far, several photonic structures have been developed in order to improve the low pair-extraction efficiency of self-assembled QDs, among which bottom-up grown nanowire QDs exhibit considerable promise. Based on the detailed studies of these sources under different excitation schemes along with understanding the effects of detection systems and multiphoton emission on the measured value of entanglement fidelity, we predict nanowire QDs can undoubtedly outperform SPDC sources, once excited via resonant TPE and detected by fast, low-noise detectors.
Admittedly, despite the fact that the results that indicate near-unity fidelity are achievable by nanowire QDs, the finite value of
Excitingly, this research shows that despite the challenges experienced thus far in generating on-demand and optimally entangled photon pairs, the results gained from resonant excitation of a nanowire QD have in fact revealed the enormous potential these sources have to outperform their predecessors. This research and the realization of optimally entangled photon pairs it offers have given quantum foundations, quantum communication, and quantum information a quantum leap forward.
The authors gratefully acknowledge the Swiss National Science Foundation, Industry Canada, Natural Sciences and Engineering Research Council of Canada (NSERC) and Transformative Quantum Technologies (TQT), for their funding and support.
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I am also a member of the team in charge for the supervision of Ph.D. students in the fields of development of silicon based planar waveguide sensor devices, study of inelastic electron tunnelling in planar tunnelling nanostructures for sensing applications and development of organotellurium(IV) compounds for semiconductor applications. I am a specialist in data analysis techniques and nanosurface structure. 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After obtaining a Master's degree in Mechanical Engineering, he continued his PhD studies in Robotics at the Vienna University of Technology. Here he worked as a robotic researcher with the university's Intelligent Manufacturing Systems Group as well as a guest researcher at various European universities, including the Swiss Federal Institute of Technology Lausanne (EPFL). During this time he published more than 20 scientific papers, gave presentations, served as a reviewer for major robotic journals and conferences and most importantly he co-founded and built the International Journal of Advanced Robotic Systems- world's first Open Access journal in the field of robotics. Starting this journal was a pivotal point in his career, since it was a pathway to founding IntechOpen - Open Access publisher focused on addressing academic researchers needs. Alex is a personification of IntechOpen key values being trusted, open and entrepreneurial. 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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