2000
Assignment of the Q y Absorbance Bands of Photosystem II Chromophores by Low-Temperature Optical Spectroscopy of Wild-Type and Mutant Reaction Centers †
Stewart D, Nixon P, Diner B, Brudvig G. Assignment of the Q y Absorbance Bands of Photosystem II Chromophores by Low-Temperature Optical Spectroscopy of Wild-Type and Mutant Reaction Centers †. Biochemistry 2000, 39: 14583-14594. PMID: 11087414, DOI: 10.1021/bi001246j.Peer-Reviewed Original ResearchMeSH KeywordsBacteriochlorophyllsBenzoquinonesCold TemperatureCyanobacteriaElectron Spin Resonance SpectroscopyFree RadicalsFreezingGlutamineHistidineLight-Harvesting Protein ComplexesMutagenesis, Site-DirectedOxidation-ReductionPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexSpectrophotometryTyrosineConceptsAbsorbance bandPhotosystem IIHydrogen bonding environmentOptical spectroscopyReaction center chromophoresRedox-active cofactorsDouble difference spectraLow temperature optical spectroscopyNumber of chromophoresRedox-active quinonesMutant reaction centersRedox stateRC chromophoresAxial ligandsCryogenic optical spectroscopyChromophore positionProtein environmentPSII preparationsSpectral assignmentsElectrochromic effectAccessory ChlElectronic structureChromophoreChromophore interactionsPhotosynthetic RCs
1992
Photooxidation 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
1988
Electron Donation in Photosystem II
Thompson L, Miller A, De Paula J, Brudvig G. Electron Donation in Photosystem II. Israel Journal Of Chemistry 1988, 28: 121-128. DOI: 10.1002/ijch.198800021.Peer-Reviewed Original ResearchElectron transfer pathwayElectron paramagnetic resonanceElectron donationTransfer pathwayElectron donorOxygen-evolving centerPS IIOptical spectroscopyPhotosystem IITime-resolved optical spectroscopyPrimary electron donorAlternate electron donorsParamagnetic resonanceEPR resultsCytochrome b 559EPR studiesCyclic electron transfer pathwaysMn sitesSpectroscopyPhotooxidationKinetic componentsPhotooxidation of chlorophyllDonorsKinetics
1980
Reactions of nitric oxide with cytochrome c oxidase.
Brudvig G, Stevens T, Chan S. Reactions of nitric oxide with cytochrome c oxidase. Biochemistry 1980, 19: 5275-85. PMID: 6255988, DOI: 10.1021/bi00564a020.Peer-Reviewed Original ResearchEvidence for the absence of photoreduction of the metal centers of cytochrome c oxidase by x-irradiation
Brudvig G, Bocian D, Gamble R, Chan S. Evidence for the absence of photoreduction of the metal centers of cytochrome c oxidase by x-irradiation. Biochimica Et Biophysica Acta 1980, 624: 78-89. PMID: 6250634, DOI: 10.1016/0005-2795(80)90227-5.Peer-Reviewed Original ResearchConceptsConventional X-ray sourceStanford Synchrotron Radiation LaboratoryX-ray absorption measurementsX-ray photonsPhotons/sX-ray fluxX-ray sourcesSynchrotron Radiation LaboratoryMetal centerOptical spectroscopyRadiation LaboratoryAbsorption measurementsElectron paramagnetic resonanceParamagnetic resonanceCytochrome c oxidasePhotonsPhotoreductionC oxidaseRadiationResonanceSpectroscopyOxidaseSourceMeasurementsFlux