2008
Redox Reactions of the Non-Heme Iron of Photosystem II: An EPR Spectroscopic Study
McEvoy J, Brudvig G. Redox Reactions of the Non-Heme Iron of Photosystem II: An EPR Spectroscopic Study. 2008, 141-144. DOI: 10.1007/978-1-4020-6709-9_32.Peer-Reviewed Original ResearchSecondary electron donorNon-heme ironElectron donorRedox activityElectron transfer reactionsEPR spectroscopic studiesProton transfer reactionsProton transfer pathwayPhotosystem IIRedox chemistryRedox reactionsEPR spectroscopySpectroscopic studiesCharge recombinationEPR quantitationQB sitePotassium ferricyanideReactionFe3Fe2IronLow temperatureAcceptor sitesDonor yieldChemistry
2003
Pulsed 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
2001
Direct electrochemistry of photosystem I
Kievit O, Brudvig G. Direct electrochemistry of photosystem I. Journal Of Electroanalytical Chemistry 2001, 497: 139-149. DOI: 10.1016/s0022-0728(00)00467-8.Peer-Reviewed Original ResearchDirect electrochemistryPhotosystem I.Primary electron donorElectrochemical signalPeak separationReduction potentialChlorophyll dimerElectron donorSolubilized membrane proteinsRange of proteinsElectrochemistryPresence of detergentPhotosystem ILiterature valuesDimersPowerful toolSeparationP700Membrane proteinsDetergents
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 kinetics
1998
A New Model of Cytochrome B-559 Function Based on the Observation of A Reversible Redox-Linked Interconversion Between Two Redox forms of Cytochrome B-559
Stewart D, Brudvig G. A New Model of Cytochrome B-559 Function Based on the Observation of A Reversible Redox-Linked Interconversion Between Two Redox forms of Cytochrome B-559. 1998, 1113-1116. DOI: 10.1007/978-94-011-3953-3_265.Peer-Reviewed Original ResearchPhotosystem IIRedox formsCyt b559Electron transfer pathwayHigh-potential formLow-potential formPSII samplesMn4 clusterElectron transferCyclic electron transferAlternate electron donorsElectron donorMidpoint potentialSample preparationExtrinsic polypeptidesCytochrome b559Heme environmentB559PhotooxidationP680B-type cytochromeInterconversionPreparation
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
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
1988
Electron Donation in Photosystem II
Thompson L, Miller A, De Paula J, Brudvig G. Electron Donation in Photosystem II. Israel Journal Of Chemistry 1988, 28: 121-128. DOI: 10.1002/ijch.198800021.Peer-Reviewed Original ResearchElectron transfer pathwayElectron paramagnetic resonanceElectron donationTransfer pathwayElectron donorOxygen-evolving centerPS IIOptical spectroscopyPhotosystem IITime-resolved optical spectroscopyPrimary electron donorAlternate electron donorsParamagnetic resonanceEPR resultsCytochrome b 559EPR studiesCyclic electron transfer pathwaysMn sitesSpectroscopyPhotooxidationKinetic componentsPhotooxidation of chlorophyllDonorsKinetics
1987
Formation of the S2 state and structure of the Mn complex in photosystem II lacking the extrinsic 33 kilodalton polypeptide
Miller A, de Paula J, Brudvig G. Formation of the S2 state and structure of the Mn complex in photosystem II lacking the extrinsic 33 kilodalton polypeptide. Photosynthesis Research 1987, 12: 205-218. PMID: 24435688, DOI: 10.1007/bf00055121.Peer-Reviewed Original ResearchS2-state multiline EPR signalState multiline EPR signalStable charge separationPSII membranesMultiline EPR signalEPR signalCharge separationManganese sitesElectron paramagnetic resonance spectroscopyUntreated PSII membranesElectron transfer eventsParamagnetic resonance spectroscopyPhotosystem II membranesMn complexesElectron donorResonance spectroscopyS2 stateReaction centersExtrinsic polypeptidesHigh yieldsMagnetic propertiesPhotosystem IISeparationTemperature rangeSpectroscopy
1986
Effect of the 17- and 23-kilodalton polypeptides, calcium, and chloride on electron transfer in photosystem II.
De Paula J, Li P, Miller A, Wu B, Brudvig G. Effect of the 17- and 23-kilodalton polypeptides, calcium, and chloride on electron transfer in photosystem II. Biochemistry 1986, 25: 6487-94. PMID: 3024710, DOI: 10.1021/bi00369a022.Peer-Reviewed Original ResearchConceptsS2-state multiline EPR signalMultiline EPR signalEPR signalPSII membranesPhotosystem II samplesS1 stateUntreated PSII membranesReaction centersElectron paramagnetic resonance measurementsChlorophyll moleculesPhotosystem II membranesStable charge separationParamagnetic resonance measurementsPhotosystem IIPSII samplesO2-evolving centerElectron transferCharge separationElectron donorNuclear hyperfine structureCytochrome b559Mn sitesResonance measurementsOxidationFraction of PSII
1985
Electron transfer in photosystem II at cryogenic temperatures.
De Paula J, Innes J, Brudvig G. Electron transfer in photosystem II at cryogenic temperatures. Biochemistry 1985, 24: 8114-20. PMID: 3004575, DOI: 10.1021/bi00348a042.Peer-Reviewed Original ResearchConceptsS2-state multiline EPR signalMultiline EPR signalElectron donationEPR signalS1 stateCytochrome b559Electron paramagnetic resonance spectroscopyParamagnetic resonance spectroscopyStable charge separationPhotosystem IIChemical oxidationChlorophyll cationElectron transferReaction center concentrationCharge separationElectron donorResonance spectroscopyS2 stateReaction centersTemperature rangeP680Signal speciesCenter concentrationB559Donation pathway