ArticleProtein science : a publication of the Protein Society2009
Fast structural dynamics in reduced and oxidized cytochrome c.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Regulation of Respiration and Apoptosis by Cytochrome c Threonine 58 Phosphorylation.Scientific reports · 2019Article
- Article
- Defining the Apoptotic Trigger: THE INTERACTION OF CYTOCHROME c AND CARDIOLIPIN.The Journal of biological chemistry · 2015Article
- Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c(552) and its b-type variant.Journal of biomolecular NMR · 2015Article
- Optimized reverse micelle surfactant system for high-resolution NMR spectroscopy of encapsulated proteins and nucleic acids dissolved in low viscosity fluids.Journal of the American Chemical Society · 2014Article
- A surprising role for conformational entropy in protein function.Topics in current chemistry · 2013Review
- The dynamical response of hen egg white lysozyme to the binding of a carbohydrate ligand.Protein science : a publication of the Protein Society · 2012Article
- Flexibility of the metal-binding region in apo-cupredoxins.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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4 authors.
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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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