2017
Linker Length-Dependent Electron-Injection Dynamics of Trimesitylporphyrins on SnO2 Films
Lee S, Regan K, Hedström S, Matula A, Chaudhuri S, Crabtree R, Batista V, Schmuttenmaer C, Brudvig G. Linker Length-Dependent Electron-Injection Dynamics of Trimesitylporphyrins on SnO2 Films. The Journal Of Physical Chemistry C 2017, 121: 22690-22699. DOI: 10.1021/acs.jpcc.7b07855.Peer-Reviewed Original ResearchDye-sensitized photoelectrochemical cellsElectron injection dynamicsPhotoelectrochemical cellsLinker lengthMetal oxide filmsMolecular photosensitizersPorphyrin coreAnchor groupsElectron acceptorInjection dynamicsLinkerSnO2 filmsOxide filmsFilmsTerphenyleneSystematic studyPhenylenePorphyrinsBiphenyleneSpectroscopyComputational modelingAcceptorPhotosensitizerSynthesisOxideAlternative Electron Acceptors for Photosystem II
Wiwczar J, Brudvig G. Alternative Electron Acceptors for Photosystem II. 2017, 51-66. DOI: 10.1007/978-3-319-48873-8_4.Peer-Reviewed Original ResearchElectron acceptorPhotosystem IIPhotochemical water oxidationElectron acceptor moleculesCobalt coordination complexesElectron acceptor sideElectron transfer pathwayRedox midpoint potentialAlternative electron transfer pathwaysCoordination complexesWater oxidationElectron transferMolecular oxygenMidpoint potentialCation exchangeExogenous electron acceptorsOxygenic photosynthetic organismsAcceptor sidePhotosynthetic electron transport chainAcceptorEnergy applicationsAlternative electron acceptorsThylakoid membranesCytochrome c.Photosynthetic organisms
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