Persistence of structure over fluctuations in biological electron-transfer reactions.
In the soft-wet environment of biomolecular electron transfer, it is possible that structural fluctuations could wash out medium-specific electronic effects on electron tunneling rates. We show that beyond a transition distance (2-3 A in water and 6-7 A in proteins), fluctuation contributions to the mean-squared donor-to-acceptor tunneling matrix element are likely to dominate over the average matrix element. Even though fluctuations dominate the tunneling mechanism at larger distances, we find that the protein fold is "remembered" by the electronic coupling, and structure remains a key determinant of electron transfer kinetics.
Balabin
Ilya A
IA
Department of Chemistry, Duke University, Durham, North Carolina 27708, USA. ilya.balabin@duke.edu
Beratan
David N
DN
Skourtis
Spiros S
SS
D001400:Azurin / Q000737:chemistry / Q000378:metabolism; D003573:Cytochrome b Group / Q000737:chemistry / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D008956:Models, Chemical; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics
D003573:Cytochrome b Group; D029968:Escherichia coli Proteins; D009211:Myoglobin; D011506:Proteins; D001400:Azurin; C017850:cytochrome b562, E coli