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• W1583570180 abstract "Abstract The aurovertin-F1 complex was used to monitor fluorescence changes of the mitochondrial adenosine triphosphatase during multi- and uni-site ATP hydrolysis. It is known that the fluorescence intensity of the complex is partially quenched by addition of ATP or Mg2+ and enhanced by ADP (Chang, T., and Penefsky, H. S. (1973) J. Biol. Chem. 248, 2746-2754). In the present study low concentrations of ATP (0.03 mM) induced a marked fluorescence quenching which was followed by a fast fluorescence recovery. This recovery could be prevented by EDTA or an ATP regenerating system. The rate of ATP hydrolysis by the aurovertin-F1 complex and the reversal of the ATP-induced fluorescence quenching were determined in these various conditions. ITP hydrolysis also resulted in fluorescence quenching that was followed by a recovery of fluorescence intensity. Under conditions for single site catalysis, fluorescence quenching was observed upon the addition of ATP. This strongly indicates that fluorescence changes in the aurovertin-F1 complex are due to the binding and hydrolysis of ATP at a catalytic site. Therefore the resulting ADP molecule bound at this catalytic site possibly induces the fluorescence recovery observed." @default.
• W1583570180 created "2016-06-24" @default.
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• W1583570180 date "1989-10-01" @default.
• W1583570180 modified "2023-10-03" @default.
• W1583570180 title "Aurovertin Fluorescence Changes of the Mitochondrial F1-ATPase during Multi- and Uni-site ATP Hydrolysis" @default.
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• W1583570180 doi "https://doi.org/10.1016/s0021-9258(18)71459-2" @default.
• W1583570180 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2529256" @default.
• W1583570180 hasPublicationYear "1989" @default.
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