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
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 spectroscopy
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 spectroscopy
1985
Active 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
1983
The Structure of the Metal Centers in Cytochrome c Oxidase
Chan S, Martin C, Wang H, Brudvig G, Stevens T. The Structure of the Metal Centers in Cytochrome c Oxidase. Nato Science Series C: 1983, 313-328. DOI: 10.1007/978-94-009-7049-6_27.Peer-Reviewed Original ResearchMetal centerLow-temperature electron paramagnetic resonance (EPR) spectroscopyElectron nuclear double resonance spectroscopyNuclear double resonance spectroscopyElectron paramagnetic resonance spectroscopyResonance spectroscopyParamagnetic resonance spectroscopyLow-temperature EPRO2 reduction siteDouble resonance spectroscopyReduction siteSpectroscopyCytochrome c oxidaseC oxidaseUnambiguous informationStructureEPRAmino acidsOxidaseOxideElucidationAcidNitric oxide