Crystallographic structures of the mitochondrial ubiquinol/cytochrome c oxidoreductase (cytochrome bc1 complex) suggest that the mechanism of quinol oxidation by the bc1 complex involves a substantial movement of the soluble head of the Rieske iron-sulfur protein (ISP) between reaction domains in cytochrome b and cytochrome c1 subunits. In this paper we report the results of steered molecular dynamics simulations inducing, through an applied torque within 1 ns, a 56°rotation of the soluble domain of ISP. For this purpose, a solvated structure of the bc1 complex in a phospholipid bilayer (a total of 206,720 atoms) was constructed. A subset of 91,061 atoms was actually simulated with 45,131 moving atoms. Point charge distributions for the force field parametrization of heme groups and the Fe2S2 cluster of the Rieske protein included in the simulated complex were determined. The simulations showed that rotation of the soluble domain of ISP is actually feasible. Several metastable conformations of the ISP during its rotation were identified and the interactions stabilizing the initial, final, and intermediate positions of the soluble head of the ISP domain were characterized. A pathway for proton conduction from the Q(o) site to the solvent via a water channel has been identified.
|Original language||English (US)|
|Number of pages||16|
|State||Published - Oct 1999|
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