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 ResearchConceptsCytochrome c oxidaseYeast cytochrome c oxidaseC oxidaseCysteine sulfurProteinBeef heartOxidaseElectron nuclear double resonance (ENDOR) spectraElectron paramagnetic resonanceSubstantial spin densityParamagnetic resonanceDouble resonance spectraBetaCuAResonance spectraCysteineSpin densityHistidine