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Resonance Raman spectroscopy of cytochrome c oxidase and electron transport particles with excitation near the Soret band
Authors:I Salmeen  L Rimai  D Gill  T Yamamoto  G Palmer  C R Hartzell  H Beinert
Affiliation:Scientific Research Staff, Ford Motor Co., Dearborn, MI 48121 USA;Biophysics Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, MI 48104 USA;Department of Biochemistry, Pennsylvania State University, University Park, PA 16802 USA;Institute for Enzyme Research, University of Wisconsin, Madison, WI 53706 USA
Abstract:We report the resonance Raman spectra of cytochrome c oxidase, both solubilized and in electron transport particles using laser excitation near the Soret band. As in the spectra of other hemoproteins, such as cytochrome c, the shape and intensity of a number of bands change when the oxidation state is varied. However, one of the hemes of solubilized cytochrome c oxidase shows redox behavior which is anomalous. Spectra of electron transport particles are dominated by cytochrome c oxidase. There are, however, definite differences between spectra of solubilized cytochrome c oxidase and electron transport particles in the oxidized states.
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