Activation of a complex of ATPase with the natural protein inhibitor in submitochondrial particles
Open Access
- 15 October 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 272 (1-2) , 145-148
- https://doi.org/10.1016/0014-5793(90)80469-y
Abstract
Almost all ATPase molecules in submitochondrial particles, isolated from beef heart mitochondria in the presence of MgATP, are in an inactive complex with the natural protein inhibitor (IF1). In de‐energized particles at high ionic strength a slow and irreversible ATPase activation is found to occur due to a dissociation of the enzyme‐inhibitor complex. The pH‐dependence of this process points out that deprotonation of IF1 molecule is an essential step in the dissociation of the complex. Zn2+ sharply accelerates ATPase activation, probably via binding with the deprotonated form of IF1. ATPase activation is completely prevented by MgATP, indicating the formation of a transient enzyme‐inhibitor complex retaining ATPase activityKeywords
This publication has 14 references indexed in Scilit:
- The complex of mitochondrial F1‐ATPase with the natural inhibitor protein is unable to catalyze single‐site ATP hydrolysisFEBS Letters, 1988
- The binding and release of the inhibitor protein are governed independently by ATP and membrane potential in ox-heart submitochondrial vesiclesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1988
- Kinetics of the release of the mitochondrial inhibitor protein. Correlation with synthesis and hydrolysis of ATPBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1988
- Regulatory role of the ATPase inhibitor protein on proton conduction by mitochondrial H+‐ATPase complexFEBS Letters, 1987
- Regulation of the mitochondrial ATP synthase/ATPase complexArchives of Biochemistry and Biophysics, 1986
- Regulation of H+-ATPases in oxidative- and photophosphorylationTrends in Biochemical Sciences, 1986
- The oxidation of sulfhydryl groups in mitochondrial F1‐ATPase decreases the rate of its inactivation by the natural protein inhibitorFEBS Letters, 1985
- Interaction between the mitochondrial ATP synthetase and ATPase inhibitor proteinFEBS Letters, 1985
- Interaction of F1-ATPase, from ox heart mitochondria with its naturally occurring inhibitor protein. Studies using radio-iodinated inhibitor proteinBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1983
- Proton-adenosinetriphosphatase complex of rat liver mitochondria: effect of energy state on its interaction with the adenosine triphosphatase inhibitory peptideBiochemistry, 1981