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
1990
Electron-transfer reactions in manganese-depleted photosystem II.
Buser C, Thompson L, Diner B, Brudvig G. Electron-transfer reactions in manganese-depleted photosystem II. Biochemistry 1990, 29: 8977-85. PMID: 2176840, DOI: 10.1021/bi00490a014.Peer-Reviewed Original ResearchConceptsMn-depleted photosystem II membranesElectron donation reactionsManganese-depleted photosystem IIElectron donationCytochrome b559Photosystem II membranesElectron paramagnetic resonance spectroscopyGlobal fitPSII samplesParamagnetic resonance spectroscopyEnergy differenceP680Room temperaturePhotosystem IIElectron transfer reactionsTime scalesLifetimeDecayFree energy differenceElectron transferRate constantsB559Resonance spectroscopySame orderRate of photooxidation
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 abilityMembraneTitrationConformationRemoval
1986
Differential scanning calorimetric studies of photosystem II: evidence for a structural role for cytochrome b559 in the oxygen-evolving complex.
Thompson L, Sturtevant J, Brudvig G. Differential scanning calorimetric studies of photosystem II: evidence for a structural role for cytochrome b559 in the oxygen-evolving complex. Biochemistry 1986, 25: 6161-9. PMID: 3790512, DOI: 10.1021/bi00368a050.Peer-Reviewed Original ResearchConceptsOxygen-evolving complexDifferential scanning calorimetryCytochrome b559Oxygen evolution activityPeak A2Photosystem IIDifferential scanning calorimetric studiesOxidation stateRelative peak areasScanning calorimetric studiesEvolution activityDSC studiesScanning calorimetryDSC tracesPeak areaC temperature rangeDegrees C temperature rangeEndothermic transitionLight-harvesting chlorophyllLow temperature shoulderDSC peakNew probeCalorimetric studiesB559PS II
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