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- W2016308087 abstract "Mitochondrial ATPase binds ADP tightly, forming inactive complexes. Dissociation of the complexes is blocked by azide. Azide inhibits neither ATP hydrolysis at high δH+ nor ATP-dependent NAD+ reduction, provided that the ADP concentration is higher than 10−4 M. At lower ADP levels, azide is inhibitory. These data suggest that in the presence of ATP δH+ prevents the fromation of one of the inactive complexes. In the absence of ATP at high δH+, azide-sensitive complexes are not formed at any ADP concentrations tested (5 × 10−7-5 × 10−4 M). The inactive E·ADP complexes can play a significant role in the regulation of ATPase in mitochondria, preventing futile ATP hydrolysis at low δH+." @default.
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- W2016308087 date "1989-08-28" @default.
- W2016308087 modified "2023-09-24" @default.
- W2016308087 title "Energization of the membrane prevents the formation of tight inactive complexes of ATPase with MgADP in submitochondrial particles" @default.
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- W2016308087 doi "https://doi.org/10.1016/0014-5793(89)81013-0" @default.
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