2015
Triplet Oxygen Evolution Catalyzed by a Biomimetic Oxomanganese Complex: Functional Role of the Carboxylate Buffer
Rivalta I, Yang K, Brudvig G, Batista V. Triplet Oxygen Evolution Catalyzed by a Biomimetic Oxomanganese Complex: Functional Role of the Carboxylate Buffer. ACS Catalysis 2015, 5: 2384-2390. DOI: 10.1021/acscatal.5b00048.Peer-Reviewed Original ResearchOxomanganese complexesTriplet oxygenOxygen evolutionWater splittingCatalytic oxygen evolutionO bond formationBiomimetic oxomanganese complexesNucleophilic water moleculeUnderlying reaction mechanismGreen plant chloroplastsPhotosynthetic oxygen evolutionWater ligandsCarboxylate ligandsInorganic coreMn complexesSuperoxo speciesNoninnocent roleCarboxylate groupsWater moleculesSubstrate waterBond formationSynthetic complexesCarboxylate buffersNucleophilic attackRedox potential
1991
Mechanism of irreversible inhibition of O2 evolution in photosystem II by Tris(hydroxymethyl)aminomethane.
Rickert K, Sears J, Beck W, Brudvig G. Mechanism of irreversible inhibition of O2 evolution in photosystem II by Tris(hydroxymethyl)aminomethane. Biochemistry 1991, 30: 7888-94. PMID: 1651110, DOI: 10.1021/bi00246a003.Peer-Reviewed Original ResearchConceptsMn complexesPSII membranesRate of reactionO2 evolutionLow-temperature electron paramagnetic resonance (EPR) spectroscopyElectron paramagnetic resonance spectroscopyElectron donation reactionsPhotosystem IIElectron donation abilityParamagnetic resonance spectroscopyOxidation stateTris treatmentResonance spectroscopyS1 stateDark reactionTriIrreversible inhibitionReactionComplexesAminesIonsO2Effect of TrisMn2Spectroscopy
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 donorPhotooxidationElectron Spin-Lattice Relaxation of the Stable Tyrosine Radical D+ in Photosystem II
Beck W, Innes J, Brudvig G. Electron Spin-Lattice Relaxation of the Stable Tyrosine Radical D+ in Photosystem II. 1990, 817-820. DOI: 10.1007/978-94-009-0511-5_188.Peer-Reviewed Original ResearchMn complexesO2-evolving centerDark stable S1 statePhotosystem IIPhotosynthetic H2O oxidationElectron paramagnetic resonance spectraRedox-active sitesWeak dipolar couplingsParamagnetic resonance spectraH2O oxidationOxidation stateTyrosine radicalsDipolar couplingsResonance spectraS0 stateS1 stateTyr-160D2 polypeptidesRelaxation propertiesSpin-lattice relaxation rateMagnetic propertiesElectron spin-lattice relaxation rateSpin-lattice relaxationComplexesRelaxation rate
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 abilityMembraneTitrationConformationRemovalMolecular 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 coreOxidation of exogenous substrates by the O2-evolving center of photosystem II and related catalytic air oxidation of secondary alcohols via a tetranuclear manganese(IV) complex.
Beck W, Sears J, Brudvig G, Kulawiec R, Crabtree* R. Oxidation of exogenous substrates by the O2-evolving center of photosystem II and related catalytic air oxidation of secondary alcohols via a tetranuclear manganese(IV) complex. Tetrahedron 1989, 45: 4903-4911. DOI: 10.1016/s0040-4020(01)85159-0.Peer-Reviewed Original ResearchMn complexesH2O oxidationOxidation stateAir oxidationStrong oxidantsSecondary alcoholsPhotosynthetic H2O oxidationPhotosystem IIS1 stateLower oxidation statesCatalytic air oxidationLight-driven generationO2 evolution activityOxidation chemistryO2-evolving centerCatalytic cycleOxidizing statePrimary aminesSecondary aminesReductive mechanismOxidationComplexesExogenous ligandsCenter actsOxidants
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 spectroscopyFormation 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