Structure and mechanism of proton‐translocating transhydrogenase

FEBS Letters

White, Scott A.¹  Jackson, J.Baz¹  Peake, Sarah J.¹ 

[1] School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK

关键词: Transhydrogenase;    Membrane protein;    Proton translocation;    X-ray structure;    Nucleotide binding;    AcPdAD+ and AcPdADH;    oxidised and reduced forms;    respectively;    of acetylpyridine adenine dinucleotide;    NAD(H);    NADP(H) and AcPdAD(H);    etc.;    indicate both the oxidised and reduced forms of a dinucleotide;   

DOI  :  10.1016/S0014-5793(99)01644-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 helices (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.

【 授权许可】

Unknown