2002
Structure-Based Kinetic Modeling of Excited-State Transfer and Trapping in Histidine-Tagged Photosystem II Core Complexes from Synechocystis †
Vassiliev S, Lee C, Brudvig G, Bruce D. Structure-Based Kinetic Modeling of Excited-State Transfer and Trapping in Histidine-Tagged Photosystem II Core Complexes from Synechocystis †. Biochemistry 2002, 41: 12236-12243. PMID: 12356326, DOI: 10.1021/bi0262597.Peer-Reviewed Original ResearchConceptsPSII core complexesFluorescence decay kineticsCharge separationRadical pairPhotosystem IIKinetic modelPhotosystem II core complexReaction centersFluorescence decayDecay kineticsII core complexesExcited-state dynamicsExcitation energy transferPrimary radical pairEnergy levelsStatic disorder modelElectron transferCharge stabilizationEnergy level modelExcited-state transferPSII preparationsStructure-based kinetic modelCore complexExponential decay componentsSimple kinetic model
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
1996
Characterization of the Reductase Domain of Rat Neuronal Nitric Oxide Synthase Generated in the Methylotrophic Yeast Pichia pastoris CALMODULIN RESPONSE IS COMPLETE WITHIN THE REDUCTASE DOMAIN ITSELF*
Gachhui R, Presta A, Bentley D, Abu-Soud H, McArthur R, Brudvig G, Ghosh D, Stuehr D. Characterization of the Reductase Domain of Rat Neuronal Nitric Oxide Synthase Generated in the Methylotrophic Yeast Pichia pastoris CALMODULIN RESPONSE IS COMPLETE WITHIN THE REDUCTASE DOMAIN ITSELF*. Journal Of Biological Chemistry 1996, 271: 20594-20602. PMID: 8702805, DOI: 10.1074/jbc.271.34.20594.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCalmodulinCalmodulin-Binding ProteinsDNA PrimersElectron Spin Resonance SpectroscopyFlavinsFlavoproteinsIsoenzymesMolecular Sequence DataNADH DehydrogenaseNeuronsNitric Oxide SynthaseOxidation-ReductionPichiaRatsRecombinant ProteinsSpectrometry, FluorescenceTryptophanConceptsElectron transferFlavin semiquinoneReductase domainNADPH-dependent flavin reductionArtificial electron acceptorsADP affinity chromatographyHeme-containing oxygenase domainCalmodulin responseNNOS reductase domainAnaerobic titrationFlavin reductionElectron acceptorNNOS reductaseFlavin-containing reductase domainReductase proteinSemiquinoneFlavinFlavin fluorescenceOxygenase domainAffinity chromatographyCytochrome c.Pure proteinCytochrome cTransferAcceptor