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

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 ex...

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Bibliographic Details
Published in:FEBS letters 1989-02, Vol.244 (2), p.268-270
Main Authors: Tushurashvili, P.R., Dekanosidze, N.Z., Inasaridze, N.P., Kekelidze, T.N., Tsartsidze, M.A., Lomsadze, B.A.
Format: Article
Language:English
Subjects:
Animals
Cattle
Kinetics
Magnesium - metabolism
Mitochondria, Heart - enzymology
Models, Theoretical
N-EM, N-ethylmaleimide
NAD - metabolism
NAD(P)H Dehydrogenase (Quinone)
NADH dehydrogenase
Oxidation-Reduction
Quinone Reductases - metabolism
Respiratory chain, Enzyme regulation
SMP, submitochondrial particles
Submitochondrial Particles - enzymology
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(89)80542-3