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

J Biol Chem. 1980 Dec 25;255(24):11637-9.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Adenosine Triphosphate / analogs & derivatives
  • Animals
  • Cattle
  • Magnetic Resonance Spectroscopy
  • Mitochondria, Heart / enzymology*
  • Oxygen Isotopes
  • Thionucleotides

Substances

  • Oxygen Isotopes
  • Thionucleotides
  • adenosine 5'-O-(3-thiotriphosphate)
  • Adenosine Triphosphate
  • Adenosine Triphosphatases