Structural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy

被引：42

作者：

Quirk, PG ^{[1
]}

Jeeves, M ^{[1
]}

Cotton, NPJ ^{[1
]}

Smith, JK ^{[1
]}

Jackson, BJ ^{[1
]}

机构：

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

来源：

FEBS LETTERS | 1999年 / 446卷 / 01期

基金：

英国惠康基金;

关键词：

transhydrogenase; NMR; nicotinamide nucleotide; model structure; Rhodospirillum rubrum;

D O I：

10.1016/S0014-5793(99)00198-2

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：

We have analysed H-1, N-15-HSQC spectra of the recombinant, NADP(H)-binding component of transhydrogenase in. the context of the emerging three dimensional structure of the protein, Chemical shift perturbations of amino acid residues following replacement of NADP(+) with NADPH mere observed in both the adenosine and nicotinamide parts of the dinucleotide binding site and in a region which straddles the protein. These observations reflect the structural changes resulting from hydride transfer. The interactions between the recombinant, NADP(H)binding component and its partner, NAD(H)-binding protein, are complicated. Helix B of the recombinant, NADP(H)-binding component may play an important role in the binding process. (C) 1999 Federation of European Biochemical Societies.

引用

页码：127 / 132

页数：6

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