Fast structural dynamics in reduced and oxidized cytochrome c.
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.
Liu
Weixia
W
Department of Biochemistry and Biophysics, Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6059, USA.
Rumbley
Jon N
JN
Englander
S Walter
SW
Wand
A Joshua
AJ
D000818:Animals; D045304:Cytochromes c / Q000737:chemistry* / Q000378:metabolism*; D006736:Horses; D009010:Monte Carlo Method; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D011487:Protein Conformation
D045304:Cytochromes c