Fast structural dynamics in reduced and oxidized cytochrome c |
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Authors: | Weixia Liu Jon N. Rumbley S. Walter Englander A. Joshua Wand |
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Affiliation: | Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104‐6059 |
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Abstract: | The sub‐nanosecond structural dynamics of reduced and oxidized cytochrome c were characterized. Dynamic properties of the protein backbone measured by amide 15N relaxation and side chains measured by the deuterium relaxation of methyl groups change little upon change in the redox state. These results imply that the solvent reorganization energy associated with electron transfer is small, consistent with previous theoretical analyses. The relative rigidity of both redox states also implies that dynamic relief of destructive electron transfer pathway interference is not operational in free cytochrome c. |
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Keywords: | protein dynamics NMR relaxation redox state electron transfer |
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