FEBS Letters | |
Energization of the membrane prevents the formation of tight inactive complexes of ATPase with MgADP in submitochondrial particles | |
Chernyak, B.V.1  Khodjaev, E.Yu.1  | |
[1] A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, Moscow 119899, USSR | |
关键词: Mitochondrial enzyme; ATPase; H+-; Enzyme-MgADP complex; Mg; Mn-SMP and S-SMP; different types of submitochondrial particles; CCCP; carbonyl cyanide m-chloro-phenylhydrazone; | |
DOI : 10.1016/0014-5793(89)81013-0 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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+.
【 授权许可】
Unknown
【 预 览 】
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