Proton and electron transfer in bacterial reaction centers.
The bacterial reaction center couples light-induced electron transfer to proton pumping across the membrane by reactions of a quinone molecule Q(B) that binds two electrons and two protons at the active site. This article reviews recent experimental work on the mechanism of the proton-coupled electron transfer and the pathways for proton transfer to the Q(B) site. The mechanism of the first electron transfer, k((1))(AB), Q(-)(A)Q(B)-->Q(A)Q(-)(B), was shown to be rate limited by conformational gating. The mechanism of the second electron transfer, k((2))(AB), was shown to involve rapid reversible proton transfer to the semiquinone followed by rate-limiting electron transfer, H(+)+Q(-)(A)Q(-)(B) ifQ(-)(A)Q(B)H-->Q(A)(Q(B)H)(-). The pathways for transfer of the first and second protons were elucidated by high-resolution X-ray crystallography as well as kinetic studies showing changes in the rate of proton transfer due to site directed mutations and metal ion binding.
Okamura
M Y
MY
University of California, San Diego, La Jolla, CA 92093-0319, USA.
Paddock
M L
ML
Graige
M S
MS
Feher
G
G
D016227:Benzoquinones / Q000737:chemistry; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004579:Electron Transport; D004583:Electrons; D007700:Kinetics; D008027:Light; D008956:Models, Chemical; D015394:Molecular Structure; D009154:Mutation; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D011522:Protons; D012242:Rhodobacter sphaeroides
D016227:Benzoquinones; D045322:Photosynthetic Reaction Center Complex Proteins; D011522:Protons; C004532:quinone