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Structural changes in the recombinant, NADP(H)‐binding component of proton translocating transhydrogenase revealed by NMR spectroscopy
Author(s) -
Quirk Philip G.,
Jeeves Mark,
Cotton Nick P.J.,
Smith John K.,
Jackson Baz J.
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00198-2
Subject(s) - nad+ kinase , recombinant dna , heteronuclear single quantum coherence spectroscopy , context (archaeology) , chemistry , nicotinamide adenine dinucleotide , binding site , biochemistry , stereochemistry , cofactor , nuclear magnetic resonance spectroscopy , enzyme , biology , paleontology , gene
We have analysed 1 H, 15 N‐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.