FEBS Letters | |
Structural changes in the recombinant, NADP(H)‐binding component of proton translocating transhydrogenase revealed by NMR spectroscopy | |
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
【 预 览 】
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RO201912020307375ZK.pdf | 313KB | download |