Abstract
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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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 5:21 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 12, 2024, 10:48 p.m.) |
Indexed | 1 month, 3 weeks ago (June 27, 2025, 6:52 a.m.) |
Issued | 37 years, 1 month ago (July 1, 1988) |
Published | 37 years, 1 month ago (July 1, 1988) |
Published Print | 37 years, 1 month ago (July 1, 1988) |
@article{Northrup_1988, title={Brownian Dynamics of Cytochrome c and Cytochrome c Peroxidase Association}, volume={241}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.2838904}, DOI={10.1126/science.2838904}, number={4861}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Northrup, Scott H. and Boles, Jeffrey O. and Reynolds, John C. L.}, year={1988}, month=jul, pages={67–70} }