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

0352273 - ÚOCHB 2011 RIV US eng J - Journal Article
de la Lande, A. - Babcock, N. S. - Řezáč, Jan - Sanders, B. C. - Salahub, D. R.
Surface residues dynamically organize water bridges to enhance electron transfer between proteins.
Proceedings of the National Academy of Sciences of the United States of America. Roč. 107, č. 26 (2010), s. 11799-11804. ISSN 0027-8424. E-ISSN 1091-6490
Institutional research plan: CEZ:AV0Z40550506
Keywords : electron transfer * pathway model * mutations
Subject RIV: CF - Physical ; Theoretical Chemistry
Impact factor: 9.771, year: 2010

In this study, we investigate the impact of structural and conformational variations on the electronic coupling between proteins methylamine dehydrogenase and amicyanin from Paracoccus denitrificans. We used molecular dynamics 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 water bridge to a “molecular breakwater” composed of several hydrophobic residues surrounding the acceptor site. When the breakwater is affected by a mutation, bulk solvent molecules disrupt the water bridge, resulting in reduced electronic coupling that is consistent with recent experimental findings.
Permanent Link: http://hdl.handle.net/11104/0191814