2013
Water oxidation chemistry of photosystem II
Brudvig G. Water oxidation chemistry of photosystem II. The FASEB Journal 2013, 27: 98.1-98.1. DOI: 10.1096/fasebj.27.1_supplement.98.1.Peer-Reviewed Original ResearchOxygen-evolving complexWater oxidation chemistryOxidation chemistryCrystal structurePhotosystem IISubstrate water moleculesRedox-active tyrosinesX-ray crystal structureFour-electron oxidationIntermediate oxidation statesSolar fuel productionSignificant side reactionsSpecific redox stateCyanobacterial photosystem IIDesign of materialsInorganic chemistryX-ray crystallographic informationRedox stateOxidation stateWater moleculesCatalytic cycleENDOR spectroscopySide reactionsChemical problemsSpectroscopic data
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
1997
Fluorescence Quenching by Chlorophyll Cations in Photosystem II †
Schweitzer R, Brudvig G. Fluorescence Quenching by Chlorophyll Cations in Photosystem II †. Biochemistry 1997, 36: 11351-11359. PMID: 9298954, DOI: 10.1021/bi9709203.Peer-Reviewed Original ResearchConceptsFluorescence quenchingPhotosystem IIElectron donorDonor sideElectron paramagnetic resonance spectroscopyRedox-active tyrosinesRedox-active centersCharge-separated stateSteady-state fluorescence quenchingParamagnetic resonance spectroscopyRedox-active componentsElectron donor sideElectron transfer pathwayCytochrome b559Redox stateFluorescence intensityO2-evolving complexPrimary electron donorReversible oxidationChlorophyll cationElectron donationFurther oxidationChlZRapid photooxidationDifferent sample preparation
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