Počet záznamů: 1
Surface residues dynamically organize water bridges to enhance electron transfer between proteins
0352273 - UOCHB-X 2011 RIV US eng J - Článek v odborném periodiku
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
Výzkumný záměr: CEZ:AV0Z40550506
Klíčová slova: electron transfer * pathway model * mutations
Kód oboru RIV: CF - Fyzikální chemie a teoretická chemie
Impakt faktor: 9.771, rok: 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.
Trvalý link: http://hdl.handle.net/11104/0191814