Unexpected stimulation of mitochondrial ADP‐ribosylation by cyanide

FEBS Letters

Masmoudi, Ahmed¹  Malviya, Anant N.¹  Mandel, Paul¹ 

[1] Centre de Neurochimie du CNRS, 5 rue Blaise Pascal, 67084 Strasbourg Cedex, France

关键词: ADP-ribosylation;    ADP-ribosyltransferase;    Mitochondria;    Cyanide;    Cu-Zn superoxide dismutase;   

DOI  :  10.1016/0014-5793(88)80190-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cyanide, the classical inhibitor of the mitochondrial respiratory chain at site III, stimulates ADP-ribosylation of a number of mitochondrial proteins, the major protein being the 50–55 kDa band. Sodium azide, sharing the same inhibitory site, does not have the same effect. Rotenone or antimycin A have no influence on mitochondrial ADP-ribosylation. Data suggest that no apparent correlation exists between oxidoreductase function and protein ADP-ribosylation. Purified nuclear poly(ADP-ribose) polymerase activity was not affected by cyanide. The cyanide effect on mitochondrial ADP-ribosylation seems intriguing and may be attributed to NAD⁺ -CN complex formation, since NAD reacts with cyanide at pH > 8 with N-substituted nicotinamide which may prevent inhibition of ADP-ribosylation.

【 授权许可】

Unknown