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Hysteretic interaction of NADH and Mg 2+ with mammalian NADH:CoQ reductase from beef heart
Author(s) -
Tushurashvili P.R.,
Dekanosidze N.Z.,
Inasaridze N.P.,
Kekelidze T.N.,
Tsartsidze M.A.,
Lomsadze B.A.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80542-3
Subject(s) - submitochondrial particle , nad+ kinase , chemistry , nadh dehydrogenase , reductase , enzyme , biochemistry , electron transfer , stereochemistry , photochemistry , protein subunit , gene
Preincubation of submitochondrial particles (SMP) from beef heart in a reaction mixture containing low concentrations of Mg 2+ induces a time lag in the NADH:oxidase activity. Preconditioning of the SMP by NADH, but not by NAD + , prevents the Mg 2+ ‐related time lag. The data obtained show that there exists a tight binding site for Mg 2+ regulating the rate of electron transfer from NADH to the natural acceptor. The ability of Mg 2+ to form a catalytically inactive complex with the enzyme is regulated by NADH.