2001
Quantifying 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 measurements
1998
Calcium Binding Studies of Photosystem II Using a Calcium-Selective Electrode †
Grove G, Brudvig G. Calcium Binding Studies of Photosystem II Using a Calcium-Selective Electrode †. Biochemistry 1998, 37: 1532-1539. PMID: 9484223, DOI: 10.1021/bi971356z.Peer-Reviewed Original ResearchA 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
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
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