Energization of the membrane prevents the formation of tight inactive complexes of ATPase with MgADP in submitochondrial particlesстатья
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Аннотация:Mitochondrial ATPase binds ADP tightly, forming inactive complexes. Dissociation of the complexes is blocked by azide. Azide inhibits neither ATP hydrolysis at high ОґОјH+ nor ATP-dependent NAD+ reduction, provided that the ADP concentration is higher than 10в€’4 M. At lower ADP levels, azide is inhibitory. These data suggest that in the presence of ATP ОґОјH+ prevents the fromation of one of the inactive complexes. In the absence of ATP at high ОґОјH+, azide-sensitive complexes are not formed at any ADP concentrations tested (5 Г— 10в€’7-5 Г— 10в€’4 M). The inactive EВ·ADP complexes can play a significant role in the regulation of ATPase in mitochondria, preventing futile ATP hydrolysis at low ОґОјH+.