Surface residues dynamically organize water bridges to enhance electron transfer between proteins.

ABSTRACT: Cellular energy production depends on electron transfer (ET) between proteins. In this theoretical study, we investigate the impact of structural and conformational variations on the electronic coupling between the redox proteins methylamine dehydrogenase and amicyanin from Paracoccus denitrificans. We used molecular dynamics simulations to generate configurations over a duration of 40 ns (sampled at 100-fs intervals) in conjunction with an ET pathway analysis to estimate the ET coupling strength of each configuration. In the wild-type complex, we find that the most frequently occurring molecular configurations afford superior electronic coupling due to the consistent presence of a water molecule hydrogen-bonded between the donor and acceptor sites. We attribute the persistence of this wat

SUBMITTER: de la Lande A 

PROVIDER: S-EPMC2900646 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature