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Science 6 November 1987:
Vol. 238. no. 4828, pp. 794 - 797
DOI: 10.1126/science.2823387
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Articles

Science, Vol 238, Issue 4828, 794-797
Copyright © 1987 by American Association for the Advancement of Science

articles

Molecular dynamics of a cytochrome c-cytochrome b5 electron transfer complex

JJ Wendoloski, JB Matthew, PC Weber, and FR Salemme

Central Research and Development Department, E. I. du Pont de Nemours and Company, Wilmington, DE 19898.

Cytochrome c and cytochrome b5 form an electrostatically associated electron transfer complex. Computer models of this and related complexes that were generated by docking the x-ray structures of the individual proteins have provided insight into the specificity and mechanism of electron transfer reactions. Previous static modeling studies were extended by molecular dynamics simulations of a cytochrome c-cytochrome b5 intermolecular complex. The simulations indicate that electrostatic interactions at the molecular interface results in a flexible association complex that samples alternative interheme geometries and molecular conformations. Many of these transient geometries appear to be more favorable for electron transfer than those formed in the initial model complex. Of particular interest is a conformational change that occurred in phenylalanine 82 of cytochrome c that allowed the phenyl side chain to bridge the two cytochrome heme groups.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)