The complex of mitochondrial F1‐ATPase with the natural inhibitor protein is unable to catalyze single‐site ATP hydrolysis
- 28 March 1988
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 230 (1-2), 163-166
- https://doi.org/10.1016/0014-5793(88)80663-x
Abstract
Interaction of mitochondrial F1-ATPase with the isolated natural inhibitor protein resulting in the inhibition of multi-site ATP hydrolysis is accompanied by the loss of activity at low ATP concentrations when single-site hydrolysis should occur. Catalytic site occupancy by [14C]nucleotides in F1-ATPase during steady-state [14C]ATP hydrolysis, which is saturated in parallel with single-site catalysis, is prevented after blocking the enzyme with the inhibitor proteinKeywords
This publication has 19 references indexed in Scilit:
- On the rate of F1‐ATPase turnover during ATP hydrolysis by the single catalytic site Evidence that hydrolysis with a slow rate of product release does not occur at the alternating active siteFEBS Letters, 1987
- .epsilon. Subunit of Escherichia coli F1-ATPase: effects on affinity for aurovertin and inhibition of product release in unisite ATP hydrolysisBiochemistry, 1987
- Steady‐state rate of F1‐ATPase turnover during ATP hydrolysis by the single catalytic siteFEBS Letters, 1987
- Regulation of the mitochondrial ATP synthase/ATPase complexArchives of Biochemistry and Biophysics, 1986
- Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondriaJournal of Molecular Biology, 1985
- Equilibrium binding of 125I-labeled adenosine triphosphatase inhibitor protein to complex V of the mitochondrial oxidative phosphorylation systemBiochemistry, 1982
- Amino acid sequence of the protein inhibitor of mitochondrial adenosine triphosphatase.Proceedings of the National Academy of Sciences, 1981
- Regulation of the Synthesis and Hydrolysis of ATP in Biological Systems: Role of Peptide Inhibitors of H+-ATPasesPublished by Elsevier ,1981
- Radiolabeling of natural adenosine triphosphatase inhibitor with phenyl[14C]isothiocyanate and study of its interaction with mitochondrial adenosine triphosphatase. Localization of inhibitor binding sites and stoichiometry of bindingBiochemistry, 1980
- Concept on the Link between Chemical and Electro-Chemical Free Energies in (NaK)-ATPase Transport FunctionPublished by Springer Nature ,1977