5 July 1989 Cytochrome C Oxidase: The Influence Of The "Open-Closed" Transition On Cytochrome A3
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Abstract
Cytochrome c oxidase is known to display a conformational transition from a "closed" to an "open" structure upon partial reduction. In the past exogenous ligand binding kinetic differences and differences in tryptophan fluorescence have been associated with this structural change. We report changes in the resonance Raman spectrum of NO-bound cytochrome as upon this transition. We detect changes in both the heme vibrational modes and in the Fe-N-0 bending mode. Furthermore, we have been able to identify a hydroxide-bound intermediate in the enzyme. Analysis of the conditions for its generation lead to the proposal that it is stable only in the open conformation of the protein. In both of these series of experiments advantage was taken of the photoreducibility of the heme groups by the incident laser beam.
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Denis L. Rousseau, Denis L. Rousseau, Yuan-chin Ching, Yuan-chin Ching, Sanghwa Han, Sanghwa Han, Massimo Sassaroli, Massimo Sassaroli, Satish Singh, Satish Singh, } "Cytochrome C Oxidase: The Influence Of The "Open-Closed" Transition On Cytochrome A3", Proc. SPIE 1055, Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology, (5 July 1989); doi: 10.1117/12.951595; https://doi.org/10.1117/12.951595
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