2005
Construction and Characterization of Genetically Modified Synechocystis sp. PCC 6803 Photosystem II Core Complexes Containing Carotenoids with Shorter π-Conjugation than β-Carotene*
Bautista J, Tracewell C, Schlodder E, Cunningham F, Brudvig G, Diner B. Construction and Characterization of Genetically Modified Synechocystis sp. PCC 6803 Photosystem II Core Complexes Containing Carotenoids with Shorter π-Conjugation than β-Carotene*. Journal Of Biological Chemistry 2005, 280: 38839-38850. PMID: 16159754, DOI: 10.1074/jbc.m504953200.Peer-Reviewed Original ResearchMeSH KeywordsBeta CaroteneCarotenoidsCationsChlorophyllChromatographyChromatography, High Pressure LiquidElectronsGene DeletionLightManganeseModels, ChemicalModels, MolecularMutationOxidation-ReductionOxidoreductasesOxygenPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexPigmentationRhodobacter capsulatusSpectrophotometrySpectrophotometry, InfraredSynechocystisTemperatureTime FactorsTyrosineConceptsPhytoene desaturase geneII core complexesDesaturase genePS II core complexesSynechocystis spCore complexPS II assemblyCarotene desaturase genePhotosystem II core complexPCC 6803Rhodobacter capsulatusWild typeMutant strainRedox functionPhotosystem IISecondary electron transfer pathwayGenesElectron transfer pathwayLight-induced formationCarotenoidsSpChlorophyllConjugated pi-electron systemPathwayComplexes
2004
Dimer-of-Dimers Model for the Oxygen-Evolving Complex of Photosystem II. Synthesis and Properties of [MnIV 4O5(terpy)4(H2O)2](ClO4)6
Chen H, Faller J, Crabtree R, Brudvig G. Dimer-of-Dimers Model for the Oxygen-Evolving Complex of Photosystem II. Synthesis and Properties of [MnIV 4O5(terpy)4(H2O)2](ClO4)6. Journal Of The American Chemical Society 2004, 126: 7345-7349. PMID: 15186173, DOI: 10.1021/ja037389l.Peer-Reviewed Original Research
2001
Carotenoid Photooxidation in Photosystem II
Tracewell C, Vrettos J, Bautista J, Frank H, Brudvig G. Carotenoid Photooxidation in Photosystem II. Archives Of Biochemistry And Biophysics 2001, 385: 61-69. PMID: 11361027, DOI: 10.1006/abbi.2000.2150.Peer-Reviewed Original ResearchConceptsPhotosystem IIElectron transfer reactionsPhotosynthetic reaction centersWater oxidationLight-harvesting pigmentsCarotenoid cationOxidizing intermediatesElectron transferRedox roleBacterial photosynthesisReaction centersPhysical methodsCationsPhotooxidationCarotenoid compositionRedoxOxidationIntermediatesAlternate pathwayCarotenoidsMinireviewReactionPhotoprotectionPossible rolePigments
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
1998
Identification of Histidine 118 in the D1 Polypeptide of Photosystem II as the Axial Ligand to Chlorophyll Z †
Stewart D, Cua A, Chisholm D, Diner B, Bocian D, Brudvig G. Identification of Histidine 118 in the D1 Polypeptide of Photosystem II as the Axial Ligand to Chlorophyll Z †. Biochemistry 1998, 37: 10040-10046. PMID: 9665709, DOI: 10.1021/bi980668e.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonanceAxial ligandsChlorophyll ZPhotosystem IIRR spectraLow-temperature electron paramagnetic resonanceWild-type Photosystem IIRedox-active tyrosinesReaction centersEfficiency of photooxidationResonance Raman spectroscopyPSII complexesIR absorbance spectraD2 polypeptidesBacterial reaction centersParamagnetic resonanceRR signatureRaman spectroscopyAccessory ChlInfrared absorbanceQuantum yieldAbsorbance bandLigandsIR excitationLow-temperature illumination
1996
Isolation and Characterization of Spinach Photosystem II Membrane-Associated Catalase and Polyphenol Oxidase †
Sheptovitsky Y, Brudvig G. Isolation and Characterization of Spinach Photosystem II Membrane-Associated Catalase and Polyphenol Oxidase †. Biochemistry 1996, 35: 16255-16263. PMID: 8973199, DOI: 10.1021/bi9613842.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsCatalaseCatechol OxidaseChloroplastsChromatography, High Pressure LiquidChromatography, Ion ExchangeCopperElectrophoresis, Polyacrylamide GelHot TemperatureIntracellular MembranesKineticsMolecular WeightOxygenOxygen ConsumptionPeptide MappingPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexSpectrophotometrySpinacia oleraceaSubstrate SpecificityConceptsPSII membranesCentre of PSIIUV-visible absorptionO2 evolution activityThylakoid membranesSpinach thylakoid membranesAnion-exchange chromatographyMembrane-associated catalaseHeme enzymesBatch adsorptionHeme catalasesMild heat treatmentHeat treatmentMolecular weightAnion-exchange beadsNative molecular weightPPOIrreversible aggregationGel filtrationFurther manipulationAdsorptionAmino acid compositionTriazoleMembraneChromatography
1982
The nature of CuA in cytochrome c oxidase.
Stevens T, Martin C, Wang H, Brudvig G, Scholes C, Chan S. The nature of CuA in cytochrome c oxidase. Journal Of Biological Chemistry 1982, 257: 12106-12113. PMID: 6288707, DOI: 10.1016/s0021-9258(18)33685-8.Peer-Reviewed Original ResearchMeSH KeywordsCopperElectron Spin Resonance SpectroscopyElectron Transport Complex IVSaccharomyces cerevisiaeSpectrophotometryConceptsCytochrome c oxidaseYeast cytochrome c oxidaseC oxidaseCysteine sulfurProteinBeef heartOxidaseElectron nuclear double resonance (ENDOR) spectraElectron paramagnetic resonanceSubstantial spin densityParamagnetic resonanceDouble resonance spectraBetaCuAResonance spectraCysteineSpin densityHistidine
1979
Cua3 of cytochrome c oxidase is not a type 1 (blue) copper
Brudvig G, Chan S. Cua3 of cytochrome c oxidase is not a type 1 (blue) copper. FEBS Letters 1979, 106: 139-141. PMID: 227722, DOI: 10.1016/0014-5793(79)80712-7.Peer-Reviewed Original Research