1H-NMR studies on nucleotide binding to the catalytic sites of bovine mitochondrial F1-ATPase.
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.
Garin
J
J
Département de Recherche Fondamentale, Centre d'Etudes Nucleaires, Grenoble, France.
Vignais
P V
PV
Gronenborn
A M
AM
Clore
G M
GM
Gao
Z
Z
Baeuerlein
E
E
D000227:Adenine Nucleotides / Q000378:metabolism*; D000244:Adenosine Diphosphate / Q000031:analogs & derivatives / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism; D000266:Adenylyl Imidodiphosphate / Q000378:metabolism; D000818:Animals; D001386:Azides / Q000378:metabolism; D001665:Binding Sites; D002417:Cattle; D008274:Magnesium / Q000494:pharmacology; D009682:Magnetic Resonance Spectroscopy; D008929:Mitochondria, Heart / Q000201:enzymology*; D008968:Molecular Conformation; D006180:Proton-Translocating ATPases / Q000378:metabolism*
D000227:Adenine Nucleotides; D001386:Azides; D000266:Adenylyl Imidodiphosphate; C017040:8-azidoadenosine 5'-triphosphate; D000244:Adenosine Diphosphate; C022295:2-azidoadenosine 3',5'-diphosphate; C042231:2-azidoadenosine 5'-triphosphate; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases; C021622:8-azidoadenosine diphosphate; D008274:Magnesium