2001
Photosynthetic Water Oxidation in Cytochromeb 559 Mutants Containing a Disrupted Heme-binding Pocket*
Morais F, Kühn K, Stewart D, Barber J, Brudvig G, Nixon P. Photosynthetic Water Oxidation in Cytochromeb 559 Mutants Containing a Disrupted Heme-binding Pocket*. Journal Of Biological Chemistry 2001, 276: 31986-31993. PMID: 11390403, DOI: 10.1074/jbc.m103935200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCarrier ProteinsChlamydomonas reinhardtiiCytochrome b GroupDNA PrimersElectron Spin Resonance SpectroscopyHeme-Binding ProteinsHemeproteinsMutagenesis, Site-DirectedMutationOxidation-ReductionPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexWaterConceptsPhotosynthetic oxygen evolutionMethionine mutantsWild typeAlpha subunitLight-saturated ratePhotosystem two complexWild-type levelsHeme of cytochromePhotosynthetic water oxidationHeme-binding pocketOxygen evolutionChloroplast mutantsPSII supercomplexesHistidine axial ligandsChlamydomonas reinhardtiiGlutamine mutantTyrosine mutantsMutantsType levelsRedox roleHemeSubunitsOxygen evolution activityTyrosineComplexes
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
1989
Directed alteration of the D1 polypeptide of photosystem II: evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor, P680.
Metz J, Nixon P, Rögner M, Brudvig G, Diner B. Directed alteration of the D1 polypeptide of photosystem II: evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor, P680. Biochemistry 1989, 28: 6960-9. PMID: 2510819, DOI: 10.1021/bi00443a028.Peer-Reviewed Original Research