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Structure and genetics of the H+-conducting F0 portion of the ATP synthase.

作者信息

Sebald W, Friedl P, Schairer H U, Hoppe J

出版信息

Ann N Y Acad Sci. 1982;402:28-44. doi: 10.1111/j.1749-6632.1982.tb25730.x.

DOI:10.1111/j.1749-6632.1982.tb25730.x
PMID:6301336
Abstract
摘要

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Ann N Y Acad Sci. 1982;402:28-44. doi: 10.1111/j.1749-6632.1982.tb25730.x.
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The DCCD-reactive aspartyl-residue of subunit C from the Escherichia coli ATP-synthase is important for the conformation of F0.来自大肠杆菌ATP合酶的C亚基的DCCD反应性天冬氨酰残基对F0的构象很重要。
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Subunit b of the membrane moiety (F0) of ATP synthase (F1F0) from Escherichia coli is indispensable for H+ translocation and binding of the water-soluble F1 moiety.来自大肠杆菌的ATP合酶（F1F0）膜部分（F0）的亚基b对于H+转运以及水溶性F1部分的结合是不可或缺的。
Proc Natl Acad Sci U S A. 1984 Dec;81(23):7279-83. doi: 10.1073/pnas.81.23.7279.

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