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

FEBS Letters

Baeuerlein, Edmund²  Garin, Jérôme³  Gao, Zhan²  Clore, G.Marius¹  Vignais, Pierre V.³  Gronenborn, Angela M.¹ 

[1] Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA;Max-Planck-Institut für Biochemie, Abteilung Membranbiochemie, D-8033 Martinsried bei München, FRG;Laboratoire de Biochimie, Département de Recherche Fondamentale, Centre d'Etudes Nucleaires, 85X, 28041 Grenoble Cedex, France

关键词: F1-ATPase;    Nucleotide;    Bound conformation;    NOE transferred;    AdoPP(NH)P;    adenosine 5′-[β;    γ-imido]triphosphate;    NOE;    nuclear Overhauser enhancement;    TRNOE;    transferred nuclear Overhauser enhancement;   

DOI  :  10.1016/0014-5793(88)81011-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown