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Science 1 July 1988:
Vol. 241. no. 4861, pp. 67 - 70
DOI: 10.1126/science.2838904
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Articles
Science, Vol 241, Issue 4861, 67-70
Copyright © 1988 by American Association for the Advancement of Science
Brownian dynamics of cytochrome c and cytochrome c peroxidase association
SH Northrup,
JO Boles,
and
JC Reynolds
Department of Chemistry, Tennessee Technological University, Cookeville 38505.
Brownian dynamics computer simulations of the diffusional association of electron transport proteins cytochrome c (cyt c) and cytochrome c peroxidase (cyt c per) were performed. A highly detailed and realistic model of the protein structures and their electrostatic interactions was used that was based on an atomic-level spatial description. Several structural features played a role in enhancing and optimizing the electron transfer efficiency of this reaction. Favorable electrostatic interactions facilitated long-lived nonspecific encounters between the proteins that allowed the severe orientational criteria for reaction to be overcome by rotational diffusion during encounters. Thus a "reduction-in-dimensionality" effect operated. The proteins achieved plausible electron transfer orientations in a multitude of electrostatically stable encounter complexes, rather than in a single dominant complex.
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