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

Academic Article

Abstract

  • 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. Copyright (C) 1999 Federation of European Biochemical Societies.
  • Published In

  • FEBS Letters  Journal
  • Digital Object Identifier (doi)

    Author List

  • Quirk PG; Jeeves M; Cotton NPJ; Smith JK; Jackson BJ
  • Start Page

  • 127
  • End Page

  • 132
  • Volume

  • 446
  • Issue

  • 1