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

Autor: Tushurashvili PR; Department of Biophysics, Tbilisi State University, USSR., Dekanosidze NZ, Inasaridze NP, Kekelidze TN, Tsartsidze MA, Lomsadze BA
Jazyk: angličtina
Zdroj: FEBS letters [FEBS Lett] 1989 Feb 27; Vol. 244 (2), pp. 268-70.
DOI: 10.1016/0014-5793(89)80542-3
Abstrakt: 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.
Databáze: MEDLINE