2023
Computing the Relative Affinity of Chlorophylls a and b to Light-Harvesting Complex II
Ranepura G, Mao J, Vermaas J, Wang J, Gisriel C, Wei R, Ortiz-Soto J, Uddin R, Amin M, Brudvig G, Gunner M. Computing the Relative Affinity of Chlorophylls a and b to Light-Harvesting Complex II. The Journal Of Physical Chemistry B 2023, 127: 10974-10986. PMID: 38097367, DOI: 10.1021/acs.jpcb.3c06273.Peer-Reviewed Original Research
2022
Structure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light
Gisriel C, Shen G, Flesher D, Kurashov V, Golbeck J, Brudvig G, Amin M, Bryant D. Structure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light. Journal Of Biological Chemistry 2022, 299: 102815. PMID: 36549647, PMCID: PMC9843442, DOI: 10.1016/j.jbc.2022.102815.Peer-Reviewed Original ResearchMeSH KeywordsAcclimatizationChlorophyllChlorophyll ACyanobacteriaLightPhotosynthesisPhotosystem I Protein ComplexPhotosystem II Protein ComplexProtein MultimerizationConceptsFar-red light photoacclimationChl dFar-red lightPhotosystem IIChl fWater-splitting enzymeEnergy transferDimeric photosystem II complexesCryo-EM structurePhotosystem II complexElectron transfer chainWater oxidationChl f moleculesDimeric complexStructure-function relationshipsPhotosynthetic machineryPsbH subunitProtein environmentMonomeric structureOxygenic photosynthesisVisible lightFormyl moietyF moleculesAccessory pigmentsTransfer chain
2011
Chloride Regulation of Enzyme Turnover: Application to the Role of Chloride in Photosystem II
Pokhrel R, McConnell IL, Brudvig GW. Chloride Regulation of Enzyme Turnover: Application to the Role of Chloride in Photosystem II. Biochemistry 2011, 50: 2725-2734. PMID: 21366335, DOI: 10.1021/bi2000388.Peer-Reviewed Original ResearchConceptsOxygen-evolving complexPhotosystem IICatalytic residuesChloride-binding siteRecent structural evidenceCyanobacterial photosystem IISalt bridgeEnzyme-substrate complexΑ-amylaseResidue crucialConformational shiftS-state cycleLys residuesCarboxylate residuesEnzyme turnoverChloride regulationResiduesD61Structural evidenceManganese clusterEnzymeBindingD1Potential mechanismsArg
2008
Quantum Mechanics/Molecular Mechanics Study of the Catalytic Cycle of Water Splitting in Photosystem II
Sproviero EM, Gascón JA, McEvoy JP, Brudvig GW, Batista VS. Quantum Mechanics/Molecular Mechanics Study of the Catalytic Cycle of Water Splitting in Photosystem II. Journal Of The American Chemical Society 2008, 130: 3428-3442. PMID: 18290643, DOI: 10.1021/ja076130q.Peer-Reviewed Original ResearchMeSH KeywordsCalciumCatalysisComputer SimulationCrystallography, X-RayCyanobacteriaManganeseModels, ChemicalModels, MolecularOxygenPhotosystem II Protein ComplexQuantum TheoryWaterConceptsSubstrate water moleculesWater moleculesMu-oxo bridgeOxygen-evolving complexWater splittingQuantum mechanics/molecular mechanics (QM/MM) hybrid methodsQuantum Mechanics/Molecular Mechanics StudySolar fuel production systemsPhotosystem IIX-ray diffraction structureMolecular mechanics studySecond coordination shellCyanobacterium Thermosynechococcus elongatusOxomanganese clusterDioxygen evolutionTerminal ligandsXRD structureCatalytic clustersCP43-R357Ligand exchangeCatalytic reactionCatalytic cycleReaction intermediatesS0 stateNucleophilic attack
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 ResearchCalciumCatalysisManganeseModels, BiologicalModels, MolecularOxidation-ReductionOxygenPhotosystem II Protein ComplexWater
2005
New Linear High-Valent Tetranuclear Manganese-Oxo Cluster Relevant to the Oxygen-Evolving Complex of Photosystem II with Oxo, Hydroxo, and Aqua Coordinated to a Single Mn(IV)
Chen, Collomb M, Duboc C, Blondin G, Rivière E, Faller J, Crabtree R, Brudvig G. New Linear High-Valent Tetranuclear Manganese-Oxo Cluster Relevant to the Oxygen-Evolving Complex of Photosystem II with Oxo, Hydroxo, and Aqua Coordinated to a Single Mn(IV). Inorganic Chemistry 2005, 44: 9567-9573. PMID: 16323946, DOI: 10.1021/ic051462m.Peer-Reviewed Original ResearchConceptsGround stateSpin statesFirst excited spin stateExcited spin statesSpin-triplet stateLarge energy gapOxygen-Evolving ComplexMn–Mn distanceDiamagnetic ground stateEnergy gapVariable-temperature magnetic susceptibility dataX-ray powder diffractionTriplet stateMagnetic susceptibility dataTetranuclear manganeseMnIV ionsGeneral Synthesis of Di-μ-oxo Dimanganese Complexes as Functional Models for the Oxygen Evolving Complex of Photosystem II
Chen H, Tagore R, Das S, Incarvito C, Faller J, Crabtree R, Brudvig G. General Synthesis of Di-μ-oxo Dimanganese Complexes as Functional Models for the Oxygen Evolving Complex of Photosystem II. Inorganic Chemistry 2005, 44: 7661-7670. PMID: 16212393, DOI: 10.1021/ic0509940.Peer-Reviewed Original ResearchMeSH KeywordsCrystallography, X-RayModels, BiologicalModels, MolecularOrganometallic CompoundsOxygenPhotosystem II Protein ComplexConceptsDimanganese complexesCatalytic activitySeries of complexesGeneral preparative methodUV-visible spectroscopyElectrospray mass spectrometryOxygen-Evolving ComplexX-ray crystallographyPhotosystem IIParent complexEPR spectroscopyOxygen-evolving activityGeneral synthesisPreparative methodLigand librariesMass spectrometryHigh product purityComplexesMn dimersSpectroscopyProduct purityPrecursorsTerpyCrystallographyOxoConstruction 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 systemPathwayComplexesResonance Raman spectroscopy of carotenoids in Photosystem II core complexes
Tracewell C, Cua A, Bocian D, Brudvig G. Resonance Raman spectroscopy of carotenoids in Photosystem II core complexes. Photosynthesis Research 2005, 83: 45-52. PMID: 16143906, DOI: 10.1007/s11120-004-2350-6.Peer-Reviewed Original ResearchMeSH KeywordsCarotenoidsCyanobacteriaPhotosystem II Protein ComplexSpectrum Analysis, RamanTemperatureConceptsII core complexesPhotosystem II core complexResonance Raman spectroscopyPS II core complexesRaman spectroscopyTrans configurationSecondary electron transfer reactionsElectron transfer reactionsMolecular wiresNeutral carotenoidsRR spectraAbsorption bandsCore complexDifference experimentsReaction centersExcitation wavelengthComplexesSpectroscopyPS IIRR resultsReactionΒ-caroteneSpectraCarotenoidsConfiguration
2004
Q-Band EPR of the S2 State of Photosystem II Confirms an S=5/2 Origin of the X-Band g=4.1 Signal
Haddy A, Lakshmi K, Brudvig G, Frank H. Q-Band EPR of the S2 State of Photosystem II Confirms an S=5/2 Origin of the X-Band g=4.1 Signal. Biophysical Journal 2004, 87: 2885-2896. PMID: 15454478, PMCID: PMC1304705, DOI: 10.1529/biophysj.104.040238.Peer-Reviewed Original ResearchMeSH KeywordsElectron Spin Resonance SpectroscopyEthanolLightMicrowavesPhotosystem II Protein ComplexConceptsSame spin systemS2 stateSpin systemsZero-field splitting valuesMiddle Kramers doubletPhotosystem IILight-induced signalsS2 oxidation stateX-bandKramers doubletX-band signalQ-band EPRPSII-enriched membrane fragmentsSplitting valuesLow-field signalMn clusterQ-bandState originEPR signalOxidation stateStateDoubletSpectraSignalsGHzRedox 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 significanceDimer-of-Dimers Model for the Oxygen-Evolving Complex of Photosystem II. Synthesis and Properties of [MnIV 4O5(terpy)4(H2O)2](ClO4)6
Chen H, Faller J, Crabtree R, Brudvig G. Dimer-of-Dimers Model for the Oxygen-Evolving Complex of Photosystem II. Synthesis and Properties of [MnIV 4O5(terpy)4(H2O)2](ClO4)6. Journal Of The American Chemical Society 2004, 126: 7345-7349. PMID: 15186173, DOI: 10.1021/ja037389l.Peer-Reviewed Original Research
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
Water oxidation chemistry of photosystem II
Vrettos J, Brudvig G. Water oxidation chemistry of photosystem II. Philosophical Transactions Of The Royal Society B Biological Sciences 2002, 357: 1395-1405. PMID: 12437878, PMCID: PMC1693042, DOI: 10.1098/rstb.2002.1136.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCalciumElectron TransportManganeseOxygenPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexProtein ConformationWaterConceptsManganese clusterProton-coupled electron transfer stepsO bond-forming stepPhotosystem IIWater oxidation chemistryBond-forming stepElectron transfer stepFour-electron oxidationTetranuclear manganese clusterOxidation chemistryWater moleculesModel chemistryO bondNucleophilic attackIon selectivityBiophysical studiesChemistryCalcium sitesOxidationSpecific roleModel systemComplexesHis190Recent studiesWaterStructure-Based Kinetic Modeling of Excited-State Transfer and Trapping in Histidine-Tagged Photosystem II Core Complexes from Synechocystis †
Vassiliev S, Lee C, Brudvig G, Bruce D. Structure-Based Kinetic Modeling of Excited-State Transfer and Trapping in Histidine-Tagged Photosystem II Core Complexes from Synechocystis †. Biochemistry 2002, 41: 12236-12243. PMID: 12356326, DOI: 10.1021/bi0262597.Peer-Reviewed Original ResearchMeSH KeywordsCyanobacteriaHistidineKineticsLight-Harvesting Protein ComplexesModels, MolecularPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexSpectrometry, FluorescenceConceptsPSII core complexesFluorescence decay kineticsCharge separationRadical pairPhotosystem IIKinetic modelPhotosystem II core complexReaction centersFluorescence decayDecay kineticsII core complexesExcited-state dynamicsExcitation energy transferPrimary radical pairEnergy levelsStatic disorder modelElectron transferCharge stabilizationEnergy level modelExcited-state transferPSII preparationsStructure-based kinetic modelCore complexExponential decay componentsSimple kinetic model
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 preparationsQuantifying the Ion Selectivity of the Ca2+ Site in Photosystem II: Evidence for Direct Involvement of Ca2+ in O2 Formation †
Vrettos J, Stone D, Brudvig G. Quantifying the Ion Selectivity of the Ca2+ Site in Photosystem II: Evidence for Direct Involvement of Ca2+ in O2 Formation †. Biochemistry 2001, 40: 7937-7945. PMID: 11425322, DOI: 10.1021/bi010679z.Peer-Reviewed Original ResearchConceptsOxygen-evolving complexTrivalent metal ionsMetal ionsPSII samplesPhotosystem IISubstrate water moleculesSmall metal ionsO2 evolutionSteady-state enzyme kineticsWater oxidationAqua ionsWater moleculesLewis acidO2 formationIonic radiusIon selectivityKcal/Monovalent ionsIonsExtrinsic polypeptidesFree energyEnzyme kineticsStructural cofactorSr2Activity measurementsPhotosynthetic 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 activityTyrosineComplexes