2024
Structure of a biohybrid photosystem I-platinum nanoparticle solar fuel catalyst
Gisriel C, Malavath T, Qiu T, Menzel J, Batista V, Brudvig G, Utschig L. Structure of a biohybrid photosystem I-platinum nanoparticle solar fuel catalyst. Nature Communications 2024, 15: 9519. PMID: 39496605, PMCID: PMC11535483, DOI: 10.1038/s41467-024-53476-y.Peer-Reviewed Original ResearchLight-driven H2 productionFuel catalystUnity quantum efficiencyPhotosynthetic biohybrid systemsPigment-protein complexesLight-driven enzymePlatinum nanoparticlesH2 productionQuantum efficiencyPhotosystem I complexCatalystChemical energyCryo-EM structureResolution cryo-EM structureBiohybrid systemsFuel productionStored solar energyPhotosystem IBiology platformReducing equivalentsMolecular basisI complexSolar energyBinding sitesStructureF-actin architecture determines the conversion of chemical energy into mechanical work
Sakamoto R, Murrell M. F-actin architecture determines the conversion of chemical energy into mechanical work. Nature Communications 2024, 15: 3444. PMID: 38658549, PMCID: PMC11043346, DOI: 10.1038/s41467-024-47593-x.Peer-Reviewed Original ResearchConceptsF-actin architectureF-actinATP consumption rateF-actin bundlesIn vitro reconstitutionDynamic cellular processesHigher ATP consumptionActin cytoskeletonFilamentous actinMyosin motorsCellular processesATP hydrolysisPurified componentsAdenosine triphosphateForce generationConversion of chemical energyATP consumptionConsumption rateActinChemical energyMyosinNetwork contractionCytoskeletonEnergetic principlesHydrolysisMapping the Oxygens in the Oxygen-Evolving Complex of Photosystem II by Their Nucleophilicity Using Quantum Descriptors
Amin M, Kaur D, Brudvig G, Brooks B. Mapping the Oxygens in the Oxygen-Evolving Complex of Photosystem II by Their Nucleophilicity Using Quantum Descriptors. Journal Of Chemical Theory And Computation 2024, 20: 1414-1422. PMID: 38306696, DOI: 10.1021/acs.jctc.3c00926.Peer-Reviewed Original ResearchConceptual density functional theoryOxygen-evolving complexQuantum descriptorsBridging oxygenSolar energy to chemical energyEnergy to chemical energyWater splitting reactionOxygen-evolving complex of photosystem IIReactivity of moleculesDensity functional theoryComplex of photosystem IIDual descriptorFukui functionsNucleophilic attackTerminal waterArtificial catalystsAtomic contributionsModel compoundsFunctional theoryReaction mechanismNucleophilesPhotosystem IIElectrophilesMn4Chemical energy
2018
High-Energy Charge-Separated States by Reductive Electron Transfer Followed by Electron Shift in the Tetraphenylethylene–Aluminum(III) Porphyrin–Fullerene Triad
Zarrabi N, Agatemor C, Lim G, Matula A, Bayard B, Batista V, D’Souza F, Poddutoori P. High-Energy Charge-Separated States by Reductive Electron Transfer Followed by Electron Shift in the Tetraphenylethylene–Aluminum(III) Porphyrin–Fullerene Triad. The Journal Of Physical Chemistry C 2018, 123: 131-143. DOI: 10.1021/acs.jpcc.8b09500.Peer-Reviewed Original ResearchCharge-separated stateCharge separationTime-resolved spectroscopic techniquesReductive electron transferCharge separated statesExcited-state propertiesReference dyadsExcited singlet stateTetraphenylethylene unitsArtificial photosynthesisSupramolecular triadElectron transferSpectroscopic techniquesCovalent bondsPorphyrin planeTetraphenylethyleneElectron migrationPhotochemical reactionsChemical energyElectron shiftSinglet stateAlPorFullerenesPorphyrinsSeparation
2013
Cell Shape Can Mediate the Spatial Organization of the Bacterial Cytoskeleton
Wang S, Wingreen NS. Cell Shape Can Mediate the Spatial Organization of the Bacterial Cytoskeleton. Biophysical Journal 2013, 104: 541-552. PMID: 23442905, PMCID: PMC3566457, DOI: 10.1016/j.bpj.2012.12.027.Peer-Reviewed Original ResearchConceptsBacterial cytoskeletonCell shapeCytoskeletal filamentsBacterial cytoskeletal proteinsRod-shaped cellsCytoskeletal proteinsCell wallCytoskeletal polymerizationCytoskeletonSpatial patterningMreBConformational transitionSpatial organizationFilament lengthSame membraneFilamentsMembraneFtsZSpatial patternsChemical energyFilament bendingProteinPatterningProper controlMicrofluidic approach
2011
Photosynthesis: Energy Conversion
Ulas G, Brudvig G. Photosynthesis: Energy Conversion. 2011 DOI: 10.1002/9781119951438.eibc0455.Peer-Reviewed Original ResearchSolar fuel productionSustainable solar fuel productionWater oxidation catalysisWater oxidation catalystsLight-driven oxidationNatural photosynthetic systemsHigh-energy chemicalsEnergy conversionCarbon dioxide reductionSolar energy conversionFuel productionArtificial photosynthesisWater oxidationRedox levelingHalf reactionOxygenic photosynthesisElectron transferCatalytic turnoverCatalytic mechanismChemical energyDirect light absorptionElectron transport machineryLight absorptionPhotosynthetic systemsLight energy capture
2009
The Role of the βDELSEED-loop of ATP Synthase*
Mnatsakanyan N, Krishnakumar AM, Suzuki T, Weber J. The Role of the βDELSEED-loop of ATP Synthase*. Journal Of Biological Chemistry 2009, 284: 11336-11345. PMID: 19246448, PMCID: PMC2670139, DOI: 10.1074/jbc.m900374200.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceATP Synthetase ComplexesBacillusBinding SitesCell MembraneEscherichia coliMitochondrial Proton-Translocating ATPasesMolecular ConformationMolecular Sequence DataMutationNucleotidesPhosphorylationProtein Structure, TertiarySequence Homology, Amino AcidConceptsWild-type enzymeATP synthaseDELSEED-loopDeletion mutantsATP hydrolysisUnique rotational mechanismTransmembrane proton gradientHelix motifRate-limiting catalytic stepTerminal domainFunctional analysisMutantsBeta subunitMembrane vesiclesATP synthesisProton gradientAmino acidsLow abundanceCatalytic stepMechanochemical couplingCatalytic siteSynthaseChemical energyEnzymeMembrane preparations
2008
Overview: Actin-Binding Protein Function and Its Relation to Disease Pathology
Krendel M, De La Cruz E. Overview: Actin-Binding Protein Function and Its Relation to Disease Pathology. Protein Reviews 2008, 65-82. DOI: 10.1007/978-0-387-71749-4_5.Peer-Reviewed Original ResearchFundamental cellular processesForm of ATPHydrolysis of ATPActin cytoskeletonProtein functionCellular processesMyosin familyMotor proteinsActin filamentsActin monomersATP moleculesCell membraneDistinct mechanismsPathogenic bacteriaGenerate movementDisease pathologyATPFilamentsForce generationMotilityCytoskeletonOrganellesChemical energyProteinActin
2005
The mechanism of photosynthetic water splitting
McEvoy J, Gascon J, Batista V, Brudvig G. The mechanism of photosynthetic water splitting. Photochemical & Photobiological Sciences 2005, 4: 940-949. PMID: 16307106, DOI: 10.1039/b506755c.Peer-Reviewed Original ResearchConceptsProtein complex photosystem IIOxygen-evolving complexWater splittingPhotosynthetic water splittingGreen plant chloroplastsMolecular mechanics calculationsPhotosynthetic light reactionsRecent experimental resultsElectron transfer pathwayX-ray crystallographic modelSource of electronsProton concentration gradientPlant chloroplastsProduct protonsMechanics calculationsOxygenic photosynthesisDioxygen gasThylakoid lumenAerobic lifeElectronsThylakoid membranesCatalytic mechanismChemical energyPhotosystem IIManganese ionsPhotosynthesis: Energy Conversion
Ulas G, Brudvig G. Photosynthesis: Energy Conversion. 2005 DOI: 10.1002/0470862106.ia805.Peer-Reviewed Original ResearchSolar fuel productionSustainable solar fuel productionWater oxidation catalysisWater oxidation catalystsLight-driven oxidationNatural photosynthetic systemsHigh-energy chemicalsEnergy conversionCarbon dioxide reductionSolar energy conversionFuel productionArtificial photosynthesisWater oxidationRedox levelingHalf reactionOxygenic photosynthesisElectron transferCatalytic turnoverCatalytic mechanismChemical energyDirect light absorptionElectron transport machineryLight absorptionPhotosynthetic systemsLight energy capture
2004
Nucleotide-dependent domain motions within rings of the RecA/AAA+ superfamily
Wang J. Nucleotide-dependent domain motions within rings of the RecA/AAA+ superfamily. Journal Of Structural Biology 2004, 148: 259-267. PMID: 15522774, DOI: 10.1016/j.jsb.2004.07.003.Peer-Reviewed Original ResearchConceptsNucleotide-dependent conformational changesT7 DNA helicaseImportant biological functionsMechanochemical motorOligomeric ringsDNA helicaseBiological functionsF1-ATPaseConformational changesDomain motionProteinMechanistic workForce generationHslUHelicaseFoldsChemical energyATPFamilyRing structureDomainMembers
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