Fast structural dynamics in reduced and oxidized cytochrome c

Weixia Liu, Jon N. Rumbley, S. Walter Englander, A. Joshua Wand

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)670-674
Number of pages5
JournalProtein Science
Issue number3
StatePublished - Mar 2009


  • Electron transfer
  • NMR relaxation
  • Protein dynamics
  • Redox state


Dive into the research topics of 'Fast structural dynamics in reduced and oxidized cytochrome c'. Together they form a unique fingerprint.

Cite this