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J. Biol. Chem., Vol. 255, Issue 24, 11637-11639, Dec, 1980

The stereochemical course of phosphoric residue transfer catalyzed by beef heart mitochondrial ATPase

MR Webb, C Grubmeyer, HS Penefsky and DR Trentham

The stereochemical course of phosphoric residue transfer has been determined for beef heart mitochondrial ATPase. When aden 5'-(3- thiotriphosphate), stereospecifically labeled with 18O in the gamma position, was hydrolyzed in [17O]water in the presence of the ATPase, the product inorganic [16O, 17O, 18O]thiophosphate was chiral. The configuration of the product showed that the hydrolysis had proceeded with inversion at the gamma-phosphorus atom. This result suggests that there is a direct, in-line transfer of the phosphoric residue between ADP and water and that there is no phosphoenzyme intermediate.
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