Interference, fluctuation, and alternation of electron tunneling in protein media. 1. Two tunneling routes in photosynthetic reaction center alternate due to thermal fluctuation of protein conformation.
Electron tunneling routes for the electron transfer from the bacteriopheophytin anion to the primary quinone in the bacterial photosynthetic reaction center of Rhodobactor sphaeroides are investigated by a combined method of molecular dynamics simulations for the protein conformation fluctuation and quantum chemical calculations for the electronic states of the donor, acceptor, and protein medium. The analysis of the tunneling route is made by mapping interatomic electron tunneling currents for each protein conformation. We found that there are two dominant routes mainly passing through Trp(M252) (Trp route) or mainly passing through Met(M218) (Met route). Actual electron tunneling pathways alternate between the two routes, depending on the protein conformation which varies with time. When either the Trp route or the Met route dominates, the electron tunneling matrix element /T(DA)/ becomes large. When both the Trp route and the Met route dominate, /T(DA)/ becomes very small due to the destructive interference of the electron tunneling currents between the two routes. We found that a linear relationship exists between the value of /T(DA)/ and the inverse of the degree of destructive interference Q for a wide range of values (ca. 3-10(3) for Q). A similar relationship was also found previously for electron transfer in ruthenium-modified azurins, suggesting that this relationship holds true in general. From these results, we are led to the conclusion that /T(DA)/ cannot exceed a maximum value at Q = 1, even if much variation of /T(DA)/ happens due to the fluctuation of protein conformation. We also conclude that the property of the electron transfer alternates between constructive and destructive interference, due to the fluctuation of protein conformation. It is impossible to keep a system in either constructive or destructive interference because thermal fluctuation of protein conformation takes place.
Nishioka
Hirotaka
H
Department of Physics, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan.
Kimura
Akihiro
A
Yamato
Takahisa
T
Kawatsu
Tsutomu
T
Kakitani
Toshiaki
T
D002627:Chemistry, Physical / Q000379:methods*; D004583:Electrons; D006358:Hot Temperature; D008956:Models, Chemical; D015233:Models, Statistical; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012242:Rhodobacter sphaeroides / Q000378:metabolism*; D013997:Time Factors; D014364:Tryptophan / Q000737:chemistry
D045322:Photosynthetic Reaction Center Complex Proteins; D011506:Proteins; D014364:Tryptophan