1984
Electron spin relaxation of CuA and cytochrome a in cytochrome c oxidase. Comparison to heme, copper, and sulfur radical complexes.
Brudvig G, Blair D, Chan S. Electron spin relaxation of CuA and cytochrome a in cytochrome c oxidase. Comparison to heme, copper, and sulfur radical complexes. Journal Of Biological Chemistry 1984, 259: 11001-11009. PMID: 6088526, DOI: 10.1016/s0021-9258(18)90613-7.Peer-Reviewed Original ResearchConceptsType 1 copperType 2 copperSulfur radicalsBlue copper proteinsMetal centerCopper complexesRadical complexesCopper centerCO complexCopper proteinsProtein environmentLow-spin heme proteinsParamagnetic sitesSpin centersHeme proteinsInorganic copperMagnetic dipolar interactionElectron spin relaxationCopperComplexesSpin-lattice relaxationDipolar interactionsCytochrome c oxidaseRadicalsCuA
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
1981
Conformations of oxidized cytochrome c oxidase.
Brudvig G, Stevens T, Morse R, Chan S. Conformations of oxidized cytochrome c oxidase. Biochemistry 1981, 20: 3912-21. PMID: 6268153, DOI: 10.1021/bi00516a039.Peer-Reviewed Original Research
1980
Reactions of nitric oxide with cytochrome c oxidase.
Brudvig G, Stevens T, Chan S. Reactions of nitric oxide with cytochrome c oxidase. Biochemistry 1980, 19: 5275-85. PMID: 6255988, DOI: 10.1021/bi00564a020.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesElectron Transport Complex IVNitric OxideOxidation-ReductionOxygenProtein BindingSpectrum AnalysisEvidence for the absence of photoreduction of the metal centers of cytochrome c oxidase by x-irradiation
Brudvig G, Bocian D, Gamble R, Chan S. Evidence for the absence of photoreduction of the metal centers of cytochrome c oxidase by x-irradiation. Biochimica Et Biophysica Acta 1980, 624: 78-89. PMID: 6250634, DOI: 10.1016/0005-2795(80)90227-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleCopperElectron Spin Resonance SpectroscopyElectron Transport Complex IVIronOxidation-ReductionParticle AcceleratorsSpectrum AnalysisTungstenConceptsConventional X-ray sourceStanford Synchrotron Radiation LaboratoryX-ray absorption measurementsX-ray photonsPhotons/sX-ray fluxX-ray sourcesSynchrotron Radiation LaboratoryMetal centerOptical spectroscopyRadiation LaboratoryAbsorption measurementsElectron paramagnetic resonanceParamagnetic resonanceCytochrome c oxidasePhotonsPhotoreductionC oxidaseRadiationResonanceSpectroscopyOxidaseSourceMeasurementsFlux
1979
Resonance Raman spectra of cytochrome c oxidase. Excitation in the 600-nm region.
Bocian D, Lemley A, Petersen N, Brudvig G, Chan S. Resonance Raman spectra of cytochrome c oxidase. Excitation in the 600-nm region. Biochemistry 1979, 18: 4396-402. PMID: 226125, DOI: 10.1021/bi00587a020.Peer-Reviewed Original ResearchCua3 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 ResearchAnimalsCattleCopperElectron Transport Complex IVMitochondria, HeartOxidation-ReductionSpectrophotometryStructure of cytochrome a3-Cua3 couple in cytochrome c oxidase as revealed by nitric oxide binding studies.
Stevens T, Brudvig G, Bocian D, Chan S. Structure of cytochrome a3-Cua3 couple in cytochrome c oxidase as revealed by nitric oxide binding studies. Proceedings Of The National Academy Of Sciences Of The United States Of America 1979, 76: 3320-3324. PMID: 226967, PMCID: PMC383817, DOI: 10.1073/pnas.76.7.3320.Peer-Reviewed Original Research