Structure and mechanism of proton-translocating transhydrogenase

被引：47

作者：

Jackson, JB ^{[1
]}

Peake, SJ ^{[1
]}

White, SA ^{[1
]}

机构：

[1] Univ Birmingham, Sch Biosci, Birmingham B15 2TT, W Midlands, England

来源：

FEBS LETTERS | 1999年 / 464卷 / 1-2期

基金：

英国惠康基金;

关键词：

transhydrogenase; membrane protein; proton translocation; x-ray structure; nucleotide binding;

D O I：

10.1016/S0014-5793(99)01644-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recent developments have led to advances in our understanding of the structure and mechanism of action of proton-translocating (or AB) transhydrogenase. There is (a) a high-resolution crystal structure, and an NMR structure, of the NADP(H)-binding component (dIII), (b) a homology-based model of the NAD(H)-binding component (dI) and (c) an emerging consensus on the position of the transmembrane heliccs (in dII), The crystal structure of dIII, in particular, provides new insights into the mechanism by which the energy released in proton translocation across the membrane is coupled to changes in the binding affinities of NADP(+) and NADPH that drive the chemical reaction. (C) 1999 Federation of European Biochemical Societies.

引用

页码：1 / 8

页数：8

共 73 条

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