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
2004
Redox 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
Structure-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
2000
Characterization 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
1998
Identification of Histidine 118 in the D1 Polypeptide of Photosystem II as the Axial Ligand to Chlorophyll Z †
Stewart D, Cua A, Chisholm D, Diner B, Bocian D, Brudvig G. Identification of Histidine 118 in the D1 Polypeptide of Photosystem II as the Axial Ligand to Chlorophyll Z †. Biochemistry 1998, 37: 10040-10046. PMID: 9665709, DOI: 10.1021/bi980668e.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonanceAxial ligandsChlorophyll ZPhotosystem IIRR spectraLow-temperature electron paramagnetic resonanceWild-type Photosystem IIRedox-active tyrosinesReaction centersEfficiency of photooxidationResonance Raman spectroscopyPSII complexesIR absorbance spectraD2 polypeptidesBacterial reaction centersParamagnetic resonanceRR signatureRaman spectroscopyAccessory ChlInfrared absorbanceQuantum yieldAbsorbance bandLigandsIR excitationLow-temperature illumination
1997
Fluorescence Quenching by Chlorophyll Cations in Photosystem II †
Schweitzer R, Brudvig G. Fluorescence Quenching by Chlorophyll Cations in Photosystem II †. Biochemistry 1997, 36: 11351-11359. PMID: 9298954, DOI: 10.1021/bi9709203.Peer-Reviewed Original ResearchConceptsFluorescence quenchingPhotosystem IIElectron donorDonor sideElectron paramagnetic resonance spectroscopyRedox-active tyrosinesRedox-active centersCharge-separated stateSteady-state fluorescence quenchingParamagnetic resonance spectroscopyRedox-active componentsElectron donor sideElectron transfer pathwayCytochrome b559Redox stateFluorescence intensityO2-evolving complexPrimary electron donorReversible oxidationChlorophyll cationElectron donationFurther oxidationChlZRapid photooxidationDifferent sample preparation
1994
Location of chlorophyllZ in photosystem II.
Koulougliotis D, Innes J, Brudvig G. Location of chlorophyllZ in photosystem II. Biochemistry 1994, 33: 11814-22. PMID: 7918399, DOI: 10.1021/bi00205a018.Peer-Reviewed Original ResearchBacteriochlorophyllsChlorophyllCold TemperatureCyanidesDarknessDysprosiumEdetic AcidElectron Spin Resonance SpectroscopyIronLightLight-Harvesting Protein ComplexesManganeseMicrowavesModels, ChemicalOxidation-ReductionPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexSpinacia oleracea
1990
Electron-transfer events leading to reconstitution of oxygen-evolution activity in manganese-depleted photosystem II membranes.
Miller A, Brudvig G. Electron-transfer events leading to reconstitution of oxygen-evolution activity in manganese-depleted photosystem II membranes. Biochemistry 1990, 29: 1385-92. PMID: 2159337, DOI: 10.1021/bi00458a007.Peer-Reviewed Original ResearchConceptsPhotooxidation of Mn2Photosystem II membranesO2 evolution activityMn complexesElectron donationMn-depleted photosystem IIPhotosystem IIElectron paramagnetic resonance spectroscopyFirst photochemical stepElectron donation reactionsCharge-separated stateElectron transfer eventsCytochrome bParamagnetic resonance spectroscopyMn-depleted photosystem II membranesOxygen evolution activityUntreated photosystem IILow quantum yieldSlower electron donationPhotochemical stepPrevious kinetic studiesTurnover reactionsElementary stepsElectron donorPhotooxidation
1989
Characterization of the multiple forms of cytochrome b559 in photosystem II.
Thompson L, Miller A, Buser C, de Paula J, Brudvig G. Characterization of the multiple forms of cytochrome b559 in photosystem II. Biochemistry 1989, 28: 8048-56. PMID: 2557895, DOI: 10.1021/bi00446a012.Peer-Reviewed Original ResearchConceptsCytochrome b559PSII membranesPhotosystem II protein complexUntreated PSII membranesExtrinsic polypeptidesLow-temperature photooxidationMn complexesPSII samplesEPR spectroscopyLigand fieldRedox titrationRedox formsEPR signalPhotosystem IIB559ComplexesThylakoid membranesPhotooxidationSpectroscopyProtein complexesUnique abilityMembraneTitrationConformationRemovalManganese and calcium requirements for reconstitution of oxygen-evolution activity in manganese-depleted photosystem II membranes.
Miller A, Brudvig G. Manganese and calcium requirements for reconstitution of oxygen-evolution activity in manganese-depleted photosystem II membranes. Biochemistry 1989, 28: 8181-90. PMID: 2557898, DOI: 10.1021/bi00446a033.Peer-Reviewed Original ResearchChloride binding to photosystem II in the dark is in slow exchange
Shachar-Hill Y, Beck W, Brudvig G. Chloride binding to photosystem II in the dark is in slow exchange. FEBS Letters 1989, 254: 184-188. PMID: 2550276, DOI: 10.1016/0014-5793(89)81035-x.Peer-Reviewed Original ResearchDirected alteration of the D1 polypeptide of photosystem II: evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor, P680.
Metz J, Nixon P, Rögner M, Brudvig G, Diner B. Directed alteration of the D1 polypeptide of photosystem II: evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor, P680. Biochemistry 1989, 28: 6960-9. PMID: 2510819, DOI: 10.1021/bi00443a028.Peer-Reviewed Original ResearchMolecular basis of the heat denaturation of photosystem II.
Thompson L, Blaylock R, Sturtevant J, Brudvig G. Molecular basis of the heat denaturation of photosystem II. Biochemistry 1989, 28: 6686-95. PMID: 2675973, DOI: 10.1021/bi00442a023.Peer-Reviewed Original ResearchMeSH KeywordsCalorimetry, Differential ScanningChlorophyllHot TemperatureLight-Harvesting Protein ComplexesManganeseOxygenPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexPlant ProteinsProtein DenaturationConceptsDifferential scanning calorimetryPSII complexesMembrane proteinsMn complexesAntenna proteinsThermal gel analysisElectron paramagnetic resonance measurementsGel analysisMembrane protein complexesMajor membrane proteinParamagnetic resonance measurementsElectron transport chainRelease of MnWater oxidationA2 peakHydroxide ionPSII membranesProtein complexesAqueous phaseComponent essentialSolubility propertiesDSC studiesMolecular basisEPR experimentsPSII coreLocation and magnetic relaxation properties of the stable tyrosine radical in photosystem II.
Innes J, Brudvig G. Location and magnetic relaxation properties of the stable tyrosine radical in photosystem II. Biochemistry 1989, 28: 1116-25. PMID: 2540815, DOI: 10.1021/bi00429a028.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsChlorophyllElectron Spin Resonance SpectroscopyFree RadicalsKineticsLight-Harvesting Protein ComplexesMathematicsMicrowavesModels, MolecularModels, TheoreticalMyoglobinPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexPlant ProteinsProtein ConformationRhodobacter sphaeroidesThermodynamicsTyrosineWhalesConceptsMetal ionsPSII membranesPhotosystem IIProtein surfaceMicrowave power saturationReaction centersRaman relaxation mechanismMagnetic relaxation propertiesFree radicalsRelaxation enhancementDipolar relaxation enhancementIonsMembrane surfaceRelaxation propertiesSpin-lattice relaxationComplexesDipolar interactionsRadicalsRhodobacter sphaeroidesProtein structureD2 subunitsPower saturationDy3Relaxation mechanismSurface
1988
Cytochrome b-559 may function to protect photosystem II from photoinhibition.
Thompson L, Brudvig G. Cytochrome b-559 may function to protect photosystem II from photoinhibition. Biochemistry 1988, 27: 6653-8. PMID: 3058202, DOI: 10.1021/bi00418a002.Peer-Reviewed Original ResearchMeSH KeywordsChlorophyllCytochrome b GroupElectron TransportLight-Harvesting Protein ComplexesOxidation-ReductionPhotochemistryPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexPlant Proteins
1987
Reactions of hydroxylamine with the electron-donor side of photosystem II.
Beck W, Brudvig G. Reactions of hydroxylamine with the electron-donor side of photosystem II. Biochemistry 1987, 26: 8285-95. PMID: 2831941, DOI: 10.1021/bi00399a040.Peer-Reviewed Original ResearchConceptsReaction of hydroxylamineMn complexesElectron donor sideO2-evolving centerCharge separationPSII membranesLow-temperature electron paramagnetic resonance (EPR) spectroscopyPhotosystem IIElectron paramagnetic resonance spectroscopyS2-state multiline EPR signalS1 stateTwo-electron reductionOne-electron photooxidationParamagnetic resonance spectroscopyN-methyl-substituted analoguesRadical oxidation productsO2 evolution activityMultiline EPR signalOxidation stateThylakoid membrane preparationsOxidation productsEvolution activityProlonged dark incubationEPR signalResonance spectroscopy