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• W2003016650 abstract "Quinone and inhibitor binding to Rhodopseudomonas sphaeroides (R-26 and GA) reaction centers were studied using spectroscopic methods and by direct adsorption of reaction centers onto anion exchange filters in the presence of 14C-labelled quinone or inhibitor. These measurements show that as secondary acceptor, QB, ubiquinone (UQ) is tightly bound in the semiquinone form and loosely bound in the quinone and quinol forms. The quinol is probably more loosely bound than the quinone. o-Phenanthroline and terbutryn, a triazine inhibitor, compete with UQ and with each other for binding to the reaction center. Inhibition by o-phenanthroline of electron transfer from the primary to the secondary quinone acceptor (QA to QB) occurs via displacement of UQ from the QB binding site. Displacement of UQ by terbutryn is apparently accessory to the inhibition of electron transfer. Terbutryn binding is lowered by reduction of QB to Q−B but is practically unaffected by reduction of QA to Q−A in the absence of QB. UQ-9 and UQ-10 have a 5- to 6-fold higher binding affinity to the QB site than does UQ-1, indicating that the long isoprenoid chain facilitates the binding to the QB site." @default.
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• W2003016650 date "1984-07-01" @default.
• W2003016650 modified "2023-09-25" @default.
• W2003016650 title "Effect of inhibitors, redox state and isoprenoid chain length on the affinity of ubiquinone for the secondary acceptor binding site in the reaction centers of photosynthetic bacteria" @default.
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• W2003016650 doi "https://doi.org/10.1016/0005-2728(84)90211-1" @default.
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