Liu Weixia, Rumbley Jon N, Englander S Walter, Wand A Joshua
Department of Biochemistry and Biophysics, Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6059, USA.
Protein Sci. 2009 Mar;18(3):670-4. doi: 10.1002/pro.72.
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.
对还原态和氧化态细胞色素c的亚纳秒级结构动力学进行了表征。通过酰胺(15)N弛豫测量的蛋白质主链动力学性质以及通过甲基的氘弛豫测量的侧链动力学性质在氧化还原状态改变时变化很小。这些结果表明,与电子转移相关的溶剂重组能很小,这与先前的理论分析一致。两种氧化还原状态的相对刚性还意味着,在游离细胞色素c中,动态缓解破坏性电子转移途径干扰不起作用。