Malyan A N
Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.
Biochemistry (Mosc). 2013 Dec;78(13):1512-23. doi: 10.1134/S0006297913130099.
ATP synthases (FoF1-ATPases) of chloroplasts, mitochondria, and bacteria catalyze ATP synthesis or hydrolysis coupled with the transmembrane transfer of protons or sodium ions. Their activity is regulated through their reversible inactivation resulting from a decreased transmembrane potential difference. The inactivation is believed to conserve ATP previously synthesized under conditions of sufficient energy supply against unproductive hydrolysis. This review is focused on the mechanism of nucleotide-dependent regulation of the ATP synthase activity where the so-called noncatalytic nucleotide binding sites are involved. Properties of these sites varying upon free enzyme transition to its membrane-bound form, their dependence on membrane energization, and putative mechanisms of noncatalytic site-mediated regulation of the ATP synthase activity are discussed.
叶绿体、线粒体和细菌中的ATP合酶（F₀F₁ - ATP酶）催化ATP的合成或水解，并伴随着质子或钠离子的跨膜转运。它们的活性通过跨膜电位差降低导致的可逆失活来调节。据信，这种失活是为了在能量供应充足的条件下，保存先前合成的ATP，防止其进行无效水解。本综述聚焦于ATP合酶活性的核苷酸依赖性调节机制，其中涉及所谓的非催化性核苷酸结合位点。讨论了这些位点在游离酶转变为膜结合形式时的性质变化、它们对膜去极化的依赖性，以及非催化位点介导的ATP合酶活性调节的推测机制。
