Hysteretic interaction of NADH and Mg2+ with mammalian NADH:CoQ reductase from beef heart

FEBS Letters

Kekelidze, T.N.¹  Tsartsidze, M.A.¹  Tushurashvili, P.R.¹  Lomsadze, B.A.¹  Inasaridze, N.P.¹  Dekanosidze, N.Z.¹ 

[1] Department of Biophysics, Tbilisi State University, Tbilisi 380038, USSR

关键词: NADH dehydrogenase;    Respiratory chain;    Enzyme regulation;    SMP;    submitochondrial particles;    N-EM;    N-ethylmaleimide;   

DOI  :  10.1016/0014-5793(89)80542-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Preincubation of submitochondrial particles (SMP) from beef heart in a reaction mixture containing low concentrations of Mg²⁺ induces a time lag in the NADH:oxidase activity. Preconditioning of the SMP by NADH, but not by NAD⁺, prevents the Mg²⁺-related time lag. The data obtained show that there exists a tight binding site for Mg²⁺ regulating the rate of electron transfer from NADH to the natural acceptor. The ability of Mg²⁺ to form a catalytically inactive complex with the enzyme is regulated by NADH.

【 授权许可】

Unknown