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Fast structural dynamics in reduced and oxidized cytochrome c

✍ Scribed by Weixia Liu; Jon N. Rumbley; S. Walter Englander; A. Joshua Wand

Book ID: 105356728
Publisher: Cold Spring Harbor Laboratory Press
Year: 2009
Tongue: English
Weight: 183 KB
Volume: 18
Category: Article
ISSN: 0961-8368
DOI: 10.1002/pro.72

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✦ Synopsis

Abstract

The sub‐nanosecond structural dynamics of reduced and oxidized cytochrome c were characterized. Dynamic properties of the protein backbone measured by amide ^15^N 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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