Fast structural dynamics in reduced and oxidized cytochrome c. Academic Article

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.

authors

• Wand, Joshua

published proceedings

• Protein Sci

author list (cited authors)

• Liu, W., Rumbley, J. N., Englander, S. W., & Wand, A. J.

citation count

• 14

complete list of authors

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

publication date

• March 2009

publisher

• Wiley  Publisher

published in

• Protein Science  Journal

keywords

• Animals
• Cytochromes C
• Horses
• Monte Carlo Method
• Nuclear Magnetic Resonance, Biomolecular
• Oxidation-Reduction
• Protein Conformation

PubMed Central ID

• 19241377

Digital Object Identifier (DOI)

• 10.1002/pro.72

start page

• 670

end page

• 674

volume

• 18

issue

• 3

URL

• http://dx.doi.org/10.1002/pro.72