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

FEBS Letters

Smith, John K.¹  Jeeves, Mark¹  Jackson, Baz J.¹  Quirk, Philip G.¹  Cotton, Nick P.J.¹ 

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

关键词: Transhydrogenase;    NMR;    Nicotinamide nucleotide;    Model structure;    Rhodospirillum rubrum;   

DOI  :  10.1016/S0014-5793(99)00198-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have analysed ¹H, ¹⁵N-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 were 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.

【 授权许可】

Unknown