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• W1896277876 abstract "The reaction mechanism of beef heart mitochondrial F1-ATPase was studied by using a fluorescent ATP analog, 2'-(5-dimethylaminonaphthalene-1-sulfonyl) amino-2'-deoxyATP (DNS-ATP), as a substrate. The following results were obtained. In the presence of Mg2+, 2 mol of DNS-ATP binds to 1 mol of F1 with an apparent dissociation constant of 0.44 μM. Upon binding, the fluorescence emission spectrum of DNS-ATP shifted to shorter wavelengths, and the fluorescence intensity at 520 nm increased 4.8-fold. On the other hand, in the absence of Mg2+, the apparent dissociation constant of F1-DNS-ATP was 16 μM, and the extent of fluorescence enhancement was 1.3- to 1.9-fold. The initial rate of fluorescence enhancement, Vf, upon addition of Mg2+ to a mixture of F1 and DNS-ATP was given by the following equation: where Vt=0.34 s−1 and Kt=3.3 μM. Following the fluorescence enhancement, TCA-P1 and free P1 were liberated consecutively. The fluorescence intensity maintained its enhanced level even after the free P1 liberation and, on addition of an excess amount of EDTA, decreased slowly to the original level. From these findings, the following reaction mechanism for F1-DNS-ATPase was proposed: where an asterisk indicates the state of bound DNS-nucleotide with enhanced fluorescence and EDNS-ADP*P is a TCA-unstable reaction intermediate. This reaction mechanism resembles that of myosin ATPase. In accordance with the reaction mechanism and the stoichiometry of DNS-ATP binding, an initial burst of TCA-P1 liberation of 2 mol/mol F1 was observed. The addition of an excess of ATP over F1-DNS-nucleotide in the presence of Mg2+ markedly accelerated the liberation of both TCA-P1 and free P1. ATP also accelerated the fluorescence decrease of F1-DNS nucleotide. Direct measurements of released free DNS-nucleotide indicated that the fluorescence decrease was due to the release of DNS-ADP from F1. ADP, AMPPNP, ITP, and GTP accelerated the F1-DNS-ATPase reaction in a similar manner. On addition of these NTPs, the release of DNS-ADP from F1 proceeded in rapid and slow steps. CTP and PP1 largely or completely failed to accelerate the conversion of EDNS-ATP* into EDNS-ADP*P. Furthermore, CTP and PP1 induced only the slow release of DNS-ADP. Therefore, we concluded that several nucleotides including ATP bind to the regulatory site{s) on F1 to induce a conformational change at the catalytic sites and accelerate each of the following steps: On the other hand, PP1 and CTP mainly accelerate the release of DNS-ADP from EDNS-ADP* by displacement. AMP did not affect the F1-DNS-ATPase reaction. The steady-state rate of F1-DNS-ATPase, v0, increased linearly with increase in the concentration of DNS-ATP and was 1 s−1 at 200 μM DNS-ATP, exceeding Vt (0.34 s−1). The time course of ATP hydrolysis after addition of ATP to F1-DNS-nucleotide showed no lag phase which corresponds to the release of DNS-ADP. These two findings indicate that F1-NTPase can also occur through a reaction path in which EpDP is not formed. P1 enhanced the fluorescence of F1-DNS-nucleotide and inhibited the displacement of bound DNS-ADP with ATP or PP1. The extent of fluorescence enhancement by P1 was maximal at 1 mol DNS-ATP/mol F1. This finding implies that the two DNS-ATP binding sites on F1 are heterogenous at least with respect to the interaction with P1." @default.
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• W1896277876 date "1981-10-01" @default.
• W1896277876 modified "2023-09-27" @default.
• W1896277876 title "Reaction Mechanism of the ATPase Activity of Mitochondrial Fi Studied by Using a Fluorescent ATP Analog, 2'-(5-Dimethyl-aminonaphthalene-1-Sulfonyl) Anuno-2'-DeoxyATP: Its Striking Resemblance to That of Myosin ATPase1" @default.
• W1896277876 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a133584" @default.
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