Noncatalytic nucleotide binding sites: Properties and mechanism of involvement in ATP synthase activity regulation View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2013-12

AUTHORS

A. N. Malyan

ABSTRACT

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. More... »

PAGES

1512-1523

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1134/s0006297913130099

    DOI

    http://dx.doi.org/10.1134/s0006297913130099

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1040120137

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/24490737


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