THE UNUSUAL ENZYMOLOGY OF ATP SYNTHASE
THE UNUSUAL ENZYMOLOGY OF ATP SYNTHASE
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DOI:
10.1021/bi00400a001
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发表时间:
1987-12-29
期刊:
影响因子:
2.9
通讯作者:
BOYER, PD
中科院分区:
文献类型:
--
作者:
BOYER, PD
From known metabolic pathways and the extent of the world’s biomass, I estimate that ATP and the ADP and P¡ from which it is formed participate in more chemical reactions than any other compounds on the earth’s surface except water. A multisubunit enzyme complex, the remarkable ATP synthase, is responsible for most of the ATP synthesis. Thisubiquitous enzyme consists of a transmembrane portion, called F0, and an attached portion, called Fv The F¡ portion when detached from the membrane acts as an ATPase. The enzyme in membranes of chloroplasts, mitochondria, and aerobic mi-croorganisms forms ATP in photophosphorylation or oxidative phosphorylation; in anaerobes the enzyme uses ATP to create a membrane potential or pH gradient. The combined efforts of many investigators, using chemical, physical, and genetic probes, have given considerable insight into the subunit composition, tertiary and quaternary structure, catalytic mechanism, and regulation of the synthase. Its structural and mechanistic characteristics are quite unusual and are thus of interest to those wanting a wider perspective of enzyme structure-function relationships as well as to the dedicated bioenergeticist. This short review gives a perspective of the structure and mechanism, of the unusual features, and of problems not yet resolved.