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Аннотация:H+-FOF1-ATP synthase (F-ATPase, F-type ATPase, FOF1-complex) catalyzes ATP synthesis from ADP and inorganic phosphate in eubacteria, mitochondria, chloroplasts and some archaea. ATP synthesis is powered by transmembrane proton transport driven by the proton-motive force (pmf) generated by the respiratory or photosynthetic electron transport chain. Upon the reduction or disappearance of the pmf ATP synthase can catalyze the reverse reaction, working as an ATP-dependent proton pump.
ATPase activity of the enzyme is regulated by several mechanisms, of which the most conservative is the non-competitive inhibition by MgADP complex (ADP-inhibition). If ADP without phosphate is bound in a catalytic site, FOF1 may undergo a conformational change that locks the bound ADP and completely inactivates the enzyme. Pmf can induce the release of the inhibitory ADP and re-activate the enzyme. In some organisms it seems that the pmf necessary for activation exceeds the level necessary for ATP synthesis. Moreover, pmf also increases the affinity of the catalytic site to phosphate, reduces the probability of ADP binding without phosphate, and thereby prevents the transition of ATP synthase into the ADP-inhibited state. Besides phosphate, some compounds including other oxyanions (e.g. sulfite), alcohols, lauryldimethylamine oxide (LDAO) and a number of other detergents can also weaken ADP-inhibition and increase the ATPase activity of the enzyme.
In this paper, we review the ADP-inhibition characteristics of ATP synthases from different organisms, discuss the role of this phenomenon in vivo and its relationship with other regulatory mechanisms - ATPase activity inhibition by subunit epsilon and nucleotide binding in the non-catalytic sites of the enzyme. We also note that in Escherichia coli enzyme the pattern of the ADP-inhibition is different: it is relatively weak and is enhanced rather than relieved by phosphate.