1H-NMR studies on nucleotide binding to the catalytic sites of bovine mitochondrial F1-ATPase

FEBS Lett. 1988 Dec 19;242(1):178-82. doi: 10.1016/0014-5793(88)81011-1.

Abstract

The conformation of adenine nucleotides bound to bovine mitochondrial F1-ATPase was investigated using transfer nuclear Overhauser enhancement measurements. It is shown that all nucleotides investigated adopt a predominantly anti conformation when bound to the catalytic sites. Furthermore, the experiment suggests that 8-azido-ADP and 8-azido-ATP, which are predominantly in the syn conformation in solution, are in the anti conformation when bound to F1 catalytic sites.

MeSH terms

  • Adenine Nucleotides / metabolism*
  • Adenosine Diphosphate / analogs & derivatives
  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphate / analogs & derivatives
  • Adenosine Triphosphate / metabolism
  • Adenylyl Imidodiphosphate / metabolism
  • Animals
  • Azides / metabolism
  • Binding Sites
  • Cattle
  • Magnesium / pharmacology
  • Magnetic Resonance Spectroscopy
  • Mitochondria, Heart / enzymology*
  • Molecular Conformation
  • Proton-Translocating ATPases / metabolism*

Substances

  • Adenine Nucleotides
  • Azides
  • Adenylyl Imidodiphosphate
  • 8-azidoadenosine 5'-triphosphate
  • Adenosine Diphosphate
  • 2-azidoadenosine 3',5'-diphosphate
  • 2-azidoadenosine 5'-triphosphate
  • Adenosine Triphosphate
  • Proton-Translocating ATPases
  • 8-azidoadenosine diphosphate
  • Magnesium