Activation of a complex of ATPase with the natural protein inhibitor in submitochondrial particlesстатья
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Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
Аннотация: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 activity