2023
Selective Methane Oxidation by Heterogenized Iridium Catalysts
Li H, Fei M, Troiano J, Ma L, Yan X, Tieu P, Yuan Y, Zhang Y, Liu T, Pan X, Brudvig G, Wang D. Selective Methane Oxidation by Heterogenized Iridium Catalysts. Journal Of The American Chemical Society 2023, 145: 769-773. PMID: 36594824, DOI: 10.1021/jacs.2c09434.Peer-Reviewed Original ResearchConceptsSelective methane oxidationValue-added oxygenatesPrepared catalystIr complexesIr centerOxide supportIridium catalystEasy separationC bondDirect CHImmobilization approachCatalystMethyl migrationOH productionMethane oxidationAcetic acidDirect routeKey stepCHCarbonylationElectrophilicityOxygenatesCarbonylBondsOxidation
2022
Highly stable preferential carbon monoxide oxidation by dinuclear heterogeneous catalysts
Zhao Y, Dai S, Yang K, Cao S, Materna K, Lant H, Kao L, Feng X, Guo J, Brudvig G, Flytzani-Stephanopoulos M, Batista V, Pan X, Wang D. Highly stable preferential carbon monoxide oxidation by dinuclear heterogeneous catalysts. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 120: e2206850120. PMID: 36577066, PMCID: PMC9910598, DOI: 10.1073/pnas.2206850120.Peer-Reviewed Original Research
2006
Water-Splitting Chemistry of Photosystem II
McEvoy JP, Brudvig GW. Water-Splitting Chemistry of Photosystem II. Chemical Reviews 2006, 106: 4455-4483. PMID: 17091926, DOI: 10.1021/cr0204294.Peer-Reviewed Original ResearchMolecular Recognition in the Selective Oxygenation of Saturated C-H Bonds by a Dimanganese Catalyst
Das S, Incarvito CD, Crabtree RH, Brudvig GW. Molecular Recognition in the Selective Oxygenation of Saturated C-H Bonds by a Dimanganese Catalyst. Science 2006, 312: 1941-1943. PMID: 16809537, DOI: 10.1126/science.1127899.Peer-Reviewed Original ResearchConceptsHydrogen bondingMolecular recognitionH bondsCarboxylic acid groupsMolecular recognition elementsSynthetic catalystsSaturated CKemp's triacidSelective oxygenationCOOH groupRegioselective functionalizationH activationHigh selectivityAcid groupsRecognition groupReactive centerRecognition elementCatalystTriacidOrient substratesSelectivityBondingBondsControl experimentsSubstrate
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 ResearchMeSH KeywordsComputer SimulationManganeseModels, MolecularOxidation-ReductionOxygenPhotosynthesisWaterConceptsProtein 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 ionsConstruction and Characterization of Genetically Modified Synechocystis sp. PCC 6803 Photosystem II Core Complexes Containing Carotenoids with Shorter π-Conjugation than β-Carotene*
Bautista J, Tracewell C, Schlodder E, Cunningham F, Brudvig G, Diner B. Construction and Characterization of Genetically Modified Synechocystis sp. PCC 6803 Photosystem II Core Complexes Containing Carotenoids with Shorter π-Conjugation than β-Carotene*. Journal Of Biological Chemistry 2005, 280: 38839-38850. PMID: 16159754, DOI: 10.1074/jbc.m504953200.Peer-Reviewed Original ResearchMeSH KeywordsBeta CaroteneCarotenoidsCationsChlorophyllChromatographyChromatography, High Pressure LiquidElectronsGene DeletionLightManganeseModels, ChemicalModels, MolecularMutationOxidation-ReductionOxidoreductasesOxygenPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexPigmentationRhodobacter capsulatusSpectrophotometrySpectrophotometry, InfraredSynechocystisTemperatureTime FactorsTyrosineConceptsPhytoene desaturase geneII core complexesDesaturase genePS II core complexesSynechocystis spCore complexPS II assemblyCarotene desaturase genePhotosystem II core complexPCC 6803Rhodobacter capsulatusWild typeMutant strainRedox functionPhotosystem IISecondary electron transfer pathwayGenesElectron transfer pathwayLight-induced formationCarotenoidsSpChlorophyllConjugated pi-electron systemPathwayComplexes
2004
The FAD-shielding Residue Phe1395 Regulates Neuronal Nitric-oxide Synthase Catalysis by Controlling NADP+ Affinity and a Conformational Equilibrium within the Flavoprotein Domain*
Konas D, Zhu K, Sharma M, Aulak K, Brudvig G, Stuehr D. The FAD-shielding Residue Phe1395 Regulates Neuronal Nitric-oxide Synthase Catalysis by Controlling NADP+ Affinity and a Conformational Equilibrium within the Flavoprotein Domain*. Journal Of Biological Chemistry 2004, 279: 35412-35425. PMID: 15180983, DOI: 10.1074/jbc.m400872200.Peer-Reviewed Original ResearchRedox Functions of Carotenoids in Photosynthesis †
Frank HA, Brudvig GW. Redox Functions of Carotenoids in Photosynthesis †. Biochemistry 2004, 43: 8607-8615. PMID: 15236568, DOI: 10.1021/bi0492096.Peer-Reviewed Original ResearchMeSH KeywordsCarotenoidsLight-Harvesting Protein ComplexesOxidation-ReductionPhotosynthesisPhotosystem II Protein ComplexConceptsBacterial light-harvesting complexesLight-harvesting complexCarotenoid cation radicalsPhotosystem IICation radicalsCation radical formationLight-harvesting pigmentsChlorophyll triplet statesPhotosynthetic reaction centersWater oxidationMolecular wiresRedox centersRedox reactionsElectron transferPhotosynthetic apparatusMeans of photoprotectionRedox roleBacterial photosynthesisRedox functionCarotenoid moleculesTriplet stateReaction centersRadical formationNovel mechanismPhysiological significance
2003
Two Redox-Active β-Carotene Molecules in Photosystem II †
Tracewell C, Brudvig G. Two Redox-Active β-Carotene Molecules in Photosystem II †. Biochemistry 2003, 42: 9127-9136. PMID: 12885246, DOI: 10.1021/bi0345844.Peer-Reviewed Original ResearchMeSH KeywordsAdaptation, PhysiologicalBeta CaroteneCyanobacteriaDarknessElectron Spin Resonance SpectroscopyFree RadicalsFreezingLight-Harvesting Protein ComplexesNormal DistributionOxidation-ReductionPhotochemistryPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexSpectroscopy, Near-InfraredSpinacia oleraceaTyrosineConceptsSecondary electron transfer pathwayElectron transfer pathwayElectron paramagnetic resonance spectroscopyElectron transfer reactionsElectron transfer pathParamagnetic resonance spectroscopyHole-hopping mechanismPS II core complexesΒ-carotene moleculesPS II membranesII core complexesPhotosystem IIIR spectroscopyPS IILow temperatureCharge separationElectrostatic interactionsOxygen evolutionResonance spectroscopyLow-temperature illuminationInhibited samplesSpectroscopyEquilibrated statePeak variesSynechocystis PCC 6803The X‐ray structure of photosystem II reveals a novel electron transport pathway between P680, cytochrome b 559 and the energy‐quenching cation, ChlZ +
Vasil’ev S, Brudvig G, Bruce D. The X‐ray structure of photosystem II reveals a novel electron transport pathway between P680, cytochrome b 559 and the energy‐quenching cation, ChlZ +. FEBS Letters 2003, 543: 159-163. PMID: 12753925, DOI: 10.1016/s0014-5793(03)00442-3.Peer-Reviewed Original ResearchPulsed High-Frequency EPR Study on the Location of Carotenoid and Chlorophyll Cation Radicals in Photosystem II
Lakshmi K, Poluektov O, Reifler M, Wagner A, Thurnauer M, Brudvig G. Pulsed High-Frequency EPR Study on the Location of Carotenoid and Chlorophyll Cation Radicals in Photosystem II. Journal Of The American Chemical Society 2003, 125: 5005-5014. PMID: 12708850, DOI: 10.1021/ja0295671.Peer-Reviewed Original ResearchMeSH KeywordsBeta CaroteneBinding SitesCationsChlorophyllCyanobacteriaDeuteriumElectron Spin Resonance SpectroscopyFerrous CompoundsFree RadicalsLight-Harvesting Protein ComplexesOxidation-ReductionPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexProtein ConformationRhodospirillumConceptsHigh-frequency EPR spectroscopyRelaxation enhancementEPR spectroscopyRelaxation ratePS IIElectron donorChlorophyll cation radicalsSpin-lattice relaxation rateWater oxidation complexFrequency EPR StudyPigment-protein complexesPhotosystem IIGreater relaxation enhancementCarotenoid-binding siteCation radicalsChlorophyll radicalsElectron transferAlternate electron donorsEPR studiesEPR signalDistance estimatesReaction centersRadicalsSpectroscopy
2002
Two New Terpyridine Dimanganese Complexes: A Manganese(III,III) Complex with a Single Unsupported Oxo Bridge and a Manganese(III,IV) Complex with a Dioxo Bridge. Synthesis, Structure, and Redox Properties
Baffert C, Collomb M, Deronzier A, Pécaut J, Limburg J, Crabtree R, Brudvig G. Two New Terpyridine Dimanganese Complexes: A Manganese(III,III) Complex with a Single Unsupported Oxo Bridge and a Manganese(III,IV) Complex with a Dioxo Bridge. Synthesis, Structure, and Redox Properties. Inorganic Chemistry 2002, 41: 1404-1411. PMID: 11896708, DOI: 10.1021/ic0107375.Peer-Reviewed Original ResearchConceptsOxo bridgeElectrochemical behaviorX-ray structureMononuclear complexesComplexes 4Oxo complexesRedox propertiesAqua complexesDimanganese complexesOrganic mediaTrans complexesCis geometrySolid stateDioxo bridgeTrans geometryCis complexesDisproportionation processTrans configurationCrystallographic formsComplexesMn atomsCisMonooxoLigandsSynthesis
2001
Factors that determine the unusually low reduction potential of cytochrome c550 in cyanobacterial photosystem II
Vrettos J, Reifler M, Kievit O, Lakshmi K, de Paula J, Brudvig G. Factors that determine the unusually low reduction potential of cytochrome c550 in cyanobacterial photosystem II. JBIC Journal Of Biological Inorganic Chemistry 2001, 6: 708-716. PMID: 11681704, DOI: 10.1007/s007750100249.Peer-Reviewed Original ResearchConceptsPCC 6803 photosystem IILow reduction potentialReduction potentialPyrolytic graphite edge electrodeElectron paramagnetic resonance spectroscopySquare wave voltammetryDirect electrochemical measurementsParamagnetic resonance spectroscopyBis-histidine axial ligationHeme reduction potentialCyanobacterial photosystem IIResonance Raman spectraPhotosystem IIWave voltammetryElectrode surfaceElectrochemistry experimentsElectrochemical measurementsElectrochemical valuesAxial ligationSolvent waterCyt c550Solvent exposureRedox titrationPeak separationPSII preparationsPhotosynthetic Water Oxidation in Cytochromeb 559 Mutants Containing a Disrupted Heme-binding Pocket*
Morais F, Kühn K, Stewart D, Barber J, Brudvig G, Nixon P. Photosynthetic Water Oxidation in Cytochromeb 559 Mutants Containing a Disrupted Heme-binding Pocket*. Journal Of Biological Chemistry 2001, 276: 31986-31993. PMID: 11390403, DOI: 10.1074/jbc.m103935200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCarrier ProteinsChlamydomonas reinhardtiiCytochrome b GroupDNA PrimersElectron Spin Resonance SpectroscopyHeme-Binding ProteinsHemeproteinsMutagenesis, Site-DirectedMutationOxidation-ReductionPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexWaterConceptsPhotosynthetic oxygen evolutionMethionine mutantsWild typeAlpha subunitLight-saturated ratePhotosystem two complexWild-type levelsHeme of cytochromePhotosynthetic water oxidationHeme-binding pocketOxygen evolutionChloroplast mutantsPSII supercomplexesHistidine axial ligandsChlamydomonas reinhardtiiGlutamine mutantTyrosine mutantsMutantsType levelsRedox roleHemeSubunitsOxygen evolution activityTyrosineComplexesCarotenoid Photooxidation in Photosystem II
Tracewell C, Vrettos J, Bautista J, Frank H, Brudvig G. Carotenoid Photooxidation in Photosystem II. Archives Of Biochemistry And Biophysics 2001, 385: 61-69. PMID: 11361027, DOI: 10.1006/abbi.2000.2150.Peer-Reviewed Original ResearchConceptsPhotosystem IIElectron transfer reactionsPhotosynthetic reaction centersWater oxidationLight-harvesting pigmentsCarotenoid cationOxidizing intermediatesElectron transferRedox roleBacterial photosynthesisReaction centersPhysical methodsCationsPhotooxidationCarotenoid compositionRedoxOxidationIntermediatesAlternate pathwayCarotenoidsMinireviewReactionPhotoprotectionPossible rolePigmentsMechanism of photosynthetic water oxidation: combining biophysical studies of photosystem II with inorganic model chemistry
Vrettos J, Limburg J, Brudvig G. Mechanism of photosynthetic water oxidation: combining biophysical studies of photosystem II with inorganic model chemistry. Biochimica Et Biophysica Acta 2001, 1503: 229-245. PMID: 11115636, DOI: 10.1016/s0005-2728(00)00214-0.Peer-Reviewed Original ResearchMeSH KeywordsCrystallographyElectron TransportHemerythrinHydrogen-Ion ConcentrationKineticsManganeseModels, ChemicalModels, MolecularOrganometallic CompoundsOxidation-ReductionOxygenPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexProtonsThylakoidsTyrosineWaterConceptsPhotosynthetic water oxidationWater oxidationOxygen-evolving complexProton-coupled electron transferTetranuclear manganese clusterMu-oxo bridgePhotosystem IIReduction of manganeseOOH speciesWater moleculesElectron transferModel chemistryManganese clusterNucleophilic attackDiferric siteFerric hydroperoxideOxidationD1 polypeptideBiophysical studiesOxyhemerythrinBiophysical resultsStructural modelDioxygenChemistryProtonation
2000
Characterization of the O2-Evolving Reaction Catalyzed by [(terpy)(H2O)MnIII(O)2MnIV(OH2)(terpy)](NO3)3 (terpy = 2,2‘:6,2‘ ‘-Terpyridine)
Limburg J, Vrettos J, Chen H, de Paula J, Crabtree R, Brudvig G. Characterization of the O2-Evolving Reaction Catalyzed by [(terpy)(H2O)MnIII(O)2MnIV(OH2)(terpy)](NO3)3 (terpy = 2,2‘:6,2‘ ‘-Terpyridine). Journal Of The American Chemical Society 2000, 123: 423-430. PMID: 11456544, DOI: 10.1021/ja001090a.Peer-Reviewed Original ResearchCharacterization of Carotenoid and Chlorophyll Photooxidation in Photosystem II †
Tracewell C, Cua A, Stewart D, Bocian D, Brudvig G. Characterization of Carotenoid and Chlorophyll Photooxidation in Photosystem II †. Biochemistry 2000, 40: 193-203. PMID: 11141071, DOI: 10.1021/bi001992o.Peer-Reviewed Original ResearchMeSH KeywordsCarotenoidsChlorophyllCyanobacteriaElectron Spin Resonance SpectroscopyFree RadicalsLight-Harvesting Protein ComplexesOxidation-ReductionPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexSpectroscopy, Near-InfraredSpectrum Analysis, RamanSpinacia oleraceaTemperatureThylakoidsConceptsSpinach PSII membranesPSII core complexesPSII membranesIR bandsElectron paramagnetic resonance spectroscopyAccessory chlorophyllPhotosystem IIParamagnetic resonance spectroscopyResonance Raman bandsPrevious spectroscopic studiesCation radicalsRaman difference spectroscopySpectroscopic studiesAlternate electron donorsElectron donorInfrared absorbanceCharacterization of carotenoidsRaman bandsResonance spectroscopyDifference spectroscopyHeme cofactorProtein conformersCore complexDifferent stabilitiesMultiphasic kineticsAssignment of the Q y Absorbance Bands of Photosystem II Chromophores by Low-Temperature Optical Spectroscopy of Wild-Type and Mutant Reaction Centers †
Stewart D, Nixon P, Diner B, Brudvig G. Assignment of the Q y Absorbance Bands of Photosystem II Chromophores by Low-Temperature Optical Spectroscopy of Wild-Type and Mutant Reaction Centers †. Biochemistry 2000, 39: 14583-14594. PMID: 11087414, DOI: 10.1021/bi001246j.Peer-Reviewed Original ResearchMeSH KeywordsBacteriochlorophyllsBenzoquinonesCold TemperatureCyanobacteriaElectron Spin Resonance SpectroscopyFree RadicalsFreezingGlutamineHistidineLight-Harvesting Protein ComplexesMutagenesis, Site-DirectedOxidation-ReductionPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexSpectrophotometryTyrosineConceptsAbsorbance bandPhotosystem IIHydrogen bonding environmentOptical spectroscopyReaction center chromophoresRedox-active cofactorsDouble difference spectraLow temperature optical spectroscopyNumber of chromophoresRedox-active quinonesMutant reaction centersRedox stateRC chromophoresAxial ligandsCryogenic optical spectroscopyChromophore positionProtein environmentPSII preparationsSpectral assignmentsElectrochromic effectAccessory ChlElectronic structureChromophoreChromophore interactionsPhotosynthetic RCs
1999
Location of the Iron−Sulfur Clusters FA and FB in Photosystem I: An Electron Paramagnetic Resonance Study of Spin Relaxation Enhancement of P700 + †
Lakshmi K, Jung Y, Golbeck J, Brudvig G. Location of the Iron−Sulfur Clusters FA and FB in Photosystem I: An Electron Paramagnetic Resonance Study of Spin Relaxation Enhancement of P700 + †. Biochemistry 1999, 38: 13210-13215. PMID: 10529193, DOI: 10.1021/bi9910777.Peer-Reviewed Original Research