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• W1996591517 endingPage "13091" @default.
• W1996591517 startingPage "13086" @default.
• W1996591517 abstract "The reaction center from Rhodobacter sphaeroides uses light energy for the reduction and protonation of a quinone molecule, Q B . This process involves the transfer of two protons from the aqueous solution to the protein-bound Q B molecule. The second proton, H + (2), is supplied to Q B by Glu-L212, an internal residue protonated in response to formation of Q A − and Q B − . In this work, the pathway for H + (2) to Glu-L212 was studied by measuring the effects of divalent metal ion binding on the protonation of Glu-L212, which was assayed by two types of processes. One was proton uptake from solution after the one-electron reduction of Q A (DQ A →D + Q A − ) and Q B (DQ B →D + Q B − ), studied by using pH-sensitive dyes. The other was the electron transfer k AB (1) (Q A − Q B →Q A Q B − ). At pH 8.5, binding of Zn 2+ , Cd 2+ , or Ni 2+ reduced the rates of proton uptake upon Q A − and Q B − formation as well as k AB (1) by ≈an order of magnitude, resulting in similar final values, indicating that there is a common rate-limiting step. Because D + Q A − is formed 10 5 -fold faster than the induced proton uptake, the observed rate decrease must be caused by an inhibition of the proton transfer. The Glu-L212→Gln mutant reaction centers displayed greatly reduced amplitudes of proton uptake and exhibited no changes in rates of proton uptake or electron transfer upon Zn 2+ binding. Therefore, metal binding specifically decreased the rate of proton transfer to Glu-L212, because the observed rates were decreased only when proton uptake by Glu-L212 was required. The entry point for the second proton H + (2) was thus identified to be the same as for the first proton H + (1), close to the metal binding region Asp-H124, His-H126, and His-H128." @default.
• W1996591517 created "2016-06-24" @default.
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• W1996591517 date "2000-11-14" @default.
• W1996591517 modified "2023-09-23" @default.
• W1996591517 title "Identification of the proton pathway in bacterial reaction centers: Both protons associated with reduction of Q _B to Q _B H ₂ share a common entry point" @default.
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• W1996591517 doi "https://doi.org/10.1073/pnas.230439597" @default.
• W1996591517 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/27182" @default.
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