Review and Hypothesis. New insights into the reaction mechanism of transhydrogenase: Swivelling the dIII component may gate the proton channel

被引：20

作者：

Jackson, J. Baz ^{[1
]}

Leung, Josephine H. ^{[2
]}

Stout, Charles D. ^{[2
]}

Schurig-Briccio, Lici A. ^{[3
]}

Gennis, Robert B. ^{[3
]}

机构：

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

[2] Scripps Res Inst, Dept Integrat Struct & Computat Biol, La Jolla, CA 92307 USA

[3] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA

来源：

FEBS LETTERS | 2015年 / 589卷 / 16期

关键词：

Transhydrogenase; Membrane-protein structure; Nicotinamide nucleotide; Proton-pump; Proton-gating; NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENASE; NADP(H)-BINDING DOMAIN III; SITE-DIRECTED MUTAGENESIS; BINDING-CHANGE MECHANISM; TRANSLOCATING TRANSHYDROGENASE; ESCHERICHIA-COLI; HYDRIDE TRANSFER; RHODOSPIRILLUM-RUBRUM; NADP(H) BINDING; BETA-SUBUNIT;

D O I：

10.1016/j.febslet.2015.06.027

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

The membrane protein transhydrogenase in animal mitochondria and bacteria couples reduction of NADP+ by NADH to proton translocation. Recent X-ray data on Thermus thermophilus transhydrogenase indicate a significant difference in the orientations of the two dIII components of the enzyme dimer (Leung et al., 2015). The character of the orientation change, and a review of information on the kinetics and thermodynamics of transhydrogenase, indicate that dill swivelling might assist in the control of proton gating by the redox state of bound NADP(+)/NADPH during enzyme turnover. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：2027 / 2033

页数：7

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