2011
Chloride Regulation of Enzyme Turnover: Application to the Role of Chloride in Photosystem II
Pokhrel R, McConnell IL, Brudvig GW. Chloride Regulation of Enzyme Turnover: Application to the Role of Chloride in Photosystem II. Biochemistry 2011, 50: 2725-2734. PMID: 21366335, DOI: 10.1021/bi2000388.Peer-Reviewed Original ResearchConceptsOxygen-evolving complexPhotosystem IICatalytic residuesChloride-binding siteRecent structural evidenceCyanobacterial photosystem IISalt bridgeEnzyme-substrate complexΑ-amylaseResidue crucialConformational shiftS-state cycleLys residuesCarboxylate residuesEnzyme turnoverChloride regulationResiduesD61Structural evidenceManganese clusterEnzymeBindingD1Potential mechanismsArg
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 ResearchConceptsDifferential 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 Research
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 spectroscopyThe tetranuclear manganese complex of Photosystem II
Brudvig G. The tetranuclear manganese complex of Photosystem II. Journal Of Bioenergetics And Biomembranes 1987, 19: 91-104. PMID: 3034873, DOI: 10.1007/bf00762719.Peer-Reviewed Original ResearchConceptsManganese complexesElectron paramagnetic resonance (EPR) spectroscopic studiesManganese ionsS2 stateTetranuclear manganese complexPhotosystem IIFour-electron oxidationIntermediate oxidation statesDisplacement of O2Coordination chemistryOxidation stateO bondSpectroscopic studiesS4 stateMagnetic propertiesComplexesIonsLike structureManganeseMn4O4ChemistryStructureBondsOxidationProperties
1986
Binding of amines to the O2-evolving center of photosystem II.
Beck W, Brudvig G. Binding of amines to the O2-evolving center of photosystem II. Biochemistry 1986, 25: 6479-86. PMID: 3024709, DOI: 10.1021/bi00369a021.Peer-Reviewed Original ResearchConceptsO2-evolving centerMultiline EPR spectrumMultiline EPR signalEPR signalS2 statePSII membranesLow-temperature electron paramagnetic resonance (EPR) spectroscopyEPR spectraElectron paramagnetic resonance spectroscopyS2-state multiline EPR signalPhotosystem IIBinding of NH3Untreated PSII membranesDirect spectroscopic evidenceParamagnetic resonance spectroscopySpinach PSII membranesMn sitesBinding of aminesDifferent EPR signalsNH3 moleculesSpectroscopic evidencePrimary aminesSteric factorsParamagnetic sitesResonance spectroscopyEffect 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 pathwayActive and resting states of the O2-evolving complex of photosystem II.
Beck W, De Paula J, Brudvig G. Active and resting states of the O2-evolving complex of photosystem II. Biochemistry 1985, 24: 3035-43. PMID: 2990539, DOI: 10.1021/bi00333a035.Peer-Reviewed Original ResearchConceptsO2-evolving complexEPR signalPSII membranesLow-temperature electron paramagnetic resonance (EPR) spectroscopyPhotosystem IIElectron paramagnetic resonance spectroscopyS2-state multiline EPR signalParamagnetic resonance spectroscopyS2 state EPR signalsMn sitesMultiline EPR signalSpinach photosystem IIThylakoid membranesCatalytic reductionChemical propertiesResonance spectroscopyDifferent hyperfine structureO2