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• W1996947208 abstract "Interprotein electron transfer (ET) reactions play an important role in biological energy conversion processes. One of these reactions, the ET between cytochrome c 2 (cyt) and reaction center from photosynthetic bacteria, is the focus of this theoretical study. The changes in the ET rate constant at fixed distances during the association process were calculated as the cyt moved from the electrostatically stabilized encounter complex to the bound state having short range van der Waals contacts in the tunneling region. Multiple conformations of the protein were generated by molecular dynamics simulations including explicit water molecules. For each of these conformations, the ET rate was calculated by using the Pathways model. The ET rate increased smoothly as the cyt approached from the encounter complex to the bound state, with a tunneling decay factor β = 1.1 Å -1 . This relatively efficient coupling between redox centers is due to the ability of interfacial water molecules to form multiple strong hydrogen bonding pathways connecting tunneling pathways on the surfaces of the two proteins. The ET rate determined for the encounter complex ensemble of states is only about a factor of 100 slower than that of the bound state (τ = 100 μs, compared with 1 μs), because of fluctuations of the cyt within the encounter complex ensemble through configurations having strong tunneling pathways. The ET rate for the encounter complex is in agreement with rates observed in mutant reaction centers modified to remove shortrange hydrophobic interactions, suggesting that in this case, ET occurs within the solvent-separated, electrostatically stabilized encounter complex." @default.
• W1996947208 created "2016-06-24" @default.
• W1996947208 creator A5030987631 @default.
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• W1996947208 date "2005-02-28" @default.
• W1996947208 modified "2023-10-11" @default.
• W1996947208 title "Interprotein electron transfer from cytochrome <i>c</i> ₂ to photosynthetic reaction center: Tunneling across an aqueous interface" @default.
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• W1996947208 doi "https://doi.org/10.1073/pnas.0409600102" @default.
• W1996947208 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/553326" @default.
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