PMID: 9526049Apr 4, 1998Paper

Unisite ATP hydrolysis by soluble Rhodospirillum rubrum F1-ATPase is accelerated by Ca2+

Biochimica Et Biophysica Acta
E Maldonado de Gómez-Puyou MT

Abstract

At saturating concentrations of ATP, soluble F1 from the Rhodospirillum rubrum (RF1) exhibits a higher rate of hydrolysis with Ca2+ than with Mg2+. The mechanisms involved in the expression of a higher catalytic activity with Ca2+ were explored by measuring the ATPase activity of RF1 at substiochiometric concentrations of ATP (unisite conditions). At a ratio of 0.25 [gamma-32P]ATP per RF1, the enzyme exhibited a 50 times higher hydrolytic rate with Ca2+ than with Mg2+. The rate of [gamma-32P]ATP binding to RF1 was in the same range with the two divalent metal ions. Centrifugation-filtration of RF1 exposed to substoichiometric [gamma-32P]ATP concentrations and Mg2+ through Sephadex columns yielded an enzyme that contained [gamma-32P]ATP and [32P]phosphate in a stoichiometry that was close to one. In the presence of Ca2+, the eluted enzyme did not contain [gamma-32P]ATP nor [32P]phosphate. This indicated that the rate of product release was faster with Ca2+ than with Mg2+. It was also observed that the ratio of multisite to unisite hydrolysis rates was of similar magnitude with both divalent cations. This suggests that they do not affect differently the cooperative mechanisms that may exist between catalytic sites. In consequence...Continue Reading

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Citations

Jun 20, 1998·The Journal of Biological Chemistry·J J García, R A Capaldi
Sep 30, 2018·Journal of Bioenergetics and Biomembranes·Francisco Mendoza-HoffmannJosé J García-Trejo

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