Kokhan O, et al. (2010) The binding interface of cytochrome c and cytochrome c in the bc complex: rationalizing the role of key residues. Biophys J 99(8):2647-56
Abstract: The interaction of cytochrome c with ubiquinol-cytochrome c oxidoreductase (bc complex) has been studied for >30 years, yet many aspects remain unclear or controversial. We report the first molecular dynamic simulations of the cyt c-bc complex interaction. Contrary to the results of crystallographic studies, our results show that there are multiple dynamic hydrogen bonds and salt bridges in the cyt c-c interface. These include most of the basic cyt c residues previously implicated in chemical modification studies. We suggest that the static nature of x-ray structures can obscure the quantitative significance of electrostatic interactions between highly mobile residues. This provides a clear resolution of the discrepancy between the structural data and functional studies. It also suggests a general need to consider dynamic interactions of charged residues in protein-protein interfaces. In addition, a novel structural change in cyt c is reported, involving residues 21-25, which may be responsible for cyt c destabilization upon binding. We also propose a mechanism of interaction between cyt c monomers responsible for limiting the binding of cyt c to only one molecule per bc dimer by altering the affinity of the cytochrome c binding site on the second cyt c monomer.CI - Copyright (c) 2010 Biophysical Society. Published by Elsevier Inc. All rights reserved.
|Status: Published||Type: Journal Article | Research Support, N.I.H., Extramural | Research Support, Non-U.S. Gov't||PubMed ID: 20959106|
Topics addressed in this paper
Number of different genes curated to this paper: 9
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