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• W1984302442 abstract "Steady-state ATP hydrolysis in the F1-ATPase of the FOF1 ATP synthase complex involves rotation of the central γ subunit relative to the catalytic sites in the α3β3 pseudo-hexamer. To understand the relationship between the catalytic mechanism and γ subunit rotation, the pre-steady-state kinetics of Mg·ATP hydrolysis in the soluble F1-ATPase upon rapid filling of all three catalytic sites was determined. The experimentally accessible partial reactions leading up to the rate-limiting step and continuing through to the steady-state mode were obtained for the first time. The burst kinetics and steady-state hydrolysis for a range of Mg·ATP concentrations provide adequate constraints for a unique minimal kinetic model that can fit all the data and satisfy extensive sensitivity tests. Significantly, the fits show that the ratio of the rates of ATP hydrolysis and synthesis is close to unity even in the steady-state mode of hydrolysis. Furthermore, the rate of Pi binding in the absence of the membranous FO sector is insignificant; thus, productive Pi binding does not occur without the influence of a proton motive force. In addition to the minimal steps of ATP binding, reversible ATP hydrolysis/synthesis, and the release of product Pi and ADP, one additional rate-limiting step is required to fit the burst kinetics. On the basis of the testing of all possible minimal kinetic models, this step must follow hydrolysis and precede Pi release in order to explain burst kinetics. Consistent with the single molecule analysis of Yasuda et al. (Yasuda, R., Noji, H., Yoshida, M., Kinosita, K., and Itoh, H. (2001) Nature 410, 898−904), we propose that the rate-limiting step involves a partial rotation of the γ subunit; hence, we name this step kγ. Moreover, the only model that is consistent with our data and many other observations in the literature suggests that reversible hydrolysis/synthesis can only occur in the active site of the βTP conformer (Abrahams, J. P., Leslie, A. G. W., Lutter, R., and Walker, J. E. (1994) Nature 370, 621−628)." @default.
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• W1984302442 date "2007-07-01" @default.
• W1984302442 modified "2023-09-26" @default.
• W1984302442 title "Determination of the Partial Reactions of Rotational Catalysis in F₁-ATPase" @default.
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• W1984302442 doi "https://doi.org/10.1021/bi700610m" @default.
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