Photoinitiated singlet and triplet electron transfer across a redesigned [myoglobin, cytochrome b5] interface.

ABSTRACT: We describe a strategy by which reactive binding of a weakly bound, 'dynamically docked (DD)' complex without a known structure can be strengthened electrostatically through optimized placement of surface charges, and discuss its use in modulating complex formation between myoglobin (Mb) and cytochrome b(5) (b(5)). The strategy employs paired Brownian dynamics (BD) simulations, one which monitors overall binding, the other reactive binding, to examine [X --> K] mutations on the surface of the partners, with a focus on single and multiple [D/E --> K] charge reversal mutations. This procedure has been applied to the [Mb, b(5)] complex, indicating mutations of Mb residues D44, D60, and E85 to be the most promising, with combinations of these showing a nonlinear enhancement of reactive binding

SUBMITTER: Nocek JM 

PROVIDER: S-EPMC2868514 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature