2003
The 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 Research
2001
Photosynthetic 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
1998
Cytochrome b559 of photosystem II
Stewart D, Brudvig G. Cytochrome b559 of photosystem II. Biochimica Et Biophysica Acta 1998, 1367: 63-87. PMID: 9784607, DOI: 10.1016/s0005-2728(98)00139-x.Peer-Reviewed Original ResearchAmino Acid SequenceChemical PhenomenaChemistry, PhysicalCytochrome b GroupElectron TransportKineticsModels, BiologicalModels, MolecularMolecular Sequence DataOxidation-ReductionPhotochemistryPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexProtein Conformation
1992
Reevaluation of the stoichiometry of cytochrome b559 in photosystem II and thylakoid membranes.
Buser C, Diner B, Brudvig G. Reevaluation of the stoichiometry of cytochrome b559 in photosystem II and thylakoid membranes. Biochemistry 1992, 31: 11441-8. PMID: 1332760, DOI: 10.1021/bi00161a024.Peer-Reviewed Original ResearchPhotooxidation of cytochrome b559 in oxygen-evolving photosystem II.
Buser C, Diner B, Brudvig G. Photooxidation of cytochrome b559 in oxygen-evolving photosystem II. Biochemistry 1992, 31: 11449-59. PMID: 1445880, DOI: 10.1021/bi00161a025.Peer-Reviewed Original ResearchConceptsCyt b559Photosystem II protein complexDark reductionOptical spectroscopyElectron transfer kineticsOxygen-evolving photosystem IIPSII-enriched membranesCytochrome b559Redox stateS2QA- charge recombinationExtent of photooxidationRate of photooxidationPrimary electron acceptorPH range 5.0Plastoquinone poolPSII samplesAcidic pH valuesRoom temperatureElectron acceptorPhotosystem IIPhotooxidationRate of reductionRedox equilibriumRange 5.0P680
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
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 Research
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 ResearchMeSH KeywordsCalorimetry, Differential ScanningCytochrome b GroupOxidation-ReductionOxygenPhotosynthesisPhotosystem II Protein ComplexPlantsConceptsOxygen-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