Resonance Raman spectroscopy of cytochrome c oxidase and electron transport particles with excitation near the Soret band |
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Authors: | I Salmeen L Rimai D Gill T Yamamoto G Palmer C R Hartzell H Beinert |
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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 |
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Abstract: | We report the resonance Raman spectra of cytochrome 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 , the shape and intensity of a number of bands change when the oxidation state is varied. However, one of the hemes of solubilized cytochrome oxidase shows redox behavior which is anomalous. Spectra of electron transport particles are dominated by cytochrome oxidase. There are, however, definite differences between spectra of solubilized cytochrome oxidase and electron transport particles in the oxidized states. |
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