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• W2060935287 endingPage "11004" @default.
• W2060935287 startingPage "10994" @default.
• W2060935287 abstract "Bacterial reaction centers (RCs) catalyze a series of electron-transfer reactions reducing a neutral quinone to a bound, anionic semiquinone. The dissociation constants and association rates of 13 tailless neutral and anionic benzo- and naphthoquinones for the Q(A) site were measured and compared. The K(d) values for these quinones range from 0.08 to 90 microM. For the eight neutral quinones, including duroquinone (DQ) and 2,3-dimethoxy-5-methyl-1,4-benzoquinone (UQ(0)), the quinone concentration and solvent viscosity dependence of the association rate indicate a second-order rate-determining step. The association rate constants (k(on)) range from 10(5) to 10(7) M(-)(1) s(-)(1). Association and dissociation rate constants were determined at pH values above the hydroxyl pK(a) for five hydroxyl naphthoquinones. These negatively charged compounds are competitive inhibitors for the Q(A) site. While the neutral quinones reach equilibrium in milliseconds, anionic hydroxyl quinones with similar K(d) values take minutes to bind or dissociate. These slow rates are independent of ionic strength, solvent viscosity, and quinone concentration, indicating a first-order rate-limiting step. The anionic semiquinone, formed by forward electron transfer at the Q(A) site, also dissociates slowly. It is not possible to measure the association rate of the unstable semiquinone. However, as the protein creates kinetic barriers for binding and releasing anionic hydroxyl quinones without greatly increasing the affinity relative to neutral quinones, it is suggested that the Q(A) site may do the same for anionic semiquinone. Thus, the slow semiquinone dissociation may not indicate significant thermodynamic stabilization of the reduced species in the Q(A) site." @default.
• W2060935287 created "2016-06-24" @default.
• W2060935287 creator A5034201179 @default.
• W2060935287 creator A5088154693 @default.
• W2060935287 date "2005-07-28" @default.
• W2060935287 modified "2023-09-24" @default.
• W2060935287 title "Modeling Binding Kinetics at the Q_A Site in Bacterial Reaction Centers" @default.
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• W2060935287 doi "https://doi.org/10.1021/bi050544j" @default.
• W2060935287 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2727067" @default.
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