Biopolym. Cell. 1991; 7(5):42-50.
Structure and Function of Biopolymers
The effect of molecular air oxygen on the enzymatic activity of NADH-dependent dehydrogenases
1Mostovnikov V. A., 1Mostovnikova G. R., 1Plavskh V. Yu., 1Tret'yakov S. A.
  1. B. I. Stepanov Institute of Physics, NAS of Belarus
    68, Nezavisimosti Avenue, Minsk, Republic of Belarus, 220072

Abstract

A new effect, the dependence of the rate of the enzymatic biochemical reaction of pyruvate transformation to lactate catalyzed by lactatedehydrogenase (LDH) in the presence of reduced nicotinamidadeninedinucleotide (NADH) on the concentration of air oxygen (O2) dissolved in the reaction medium, are reported. It is shoun that this effect is due to the dinucleotide with molecules O2 complex formation. It is found that the molecular oxygen removal from the coenzyme solution lead to the NADH spatial structure change. Changes, induced by molecular oxygen, are reversible. The dependence of the rate enzymatic biochemical reaction on concentration of dissolved oxygen has not been observed in the case of lactate-pyruvate transformation reaction catalysed by LDH in the presence of nicotinamidadeninedinucleotide (NAD+). There have not been observed the NAD+ with O2 molecules complexes formation.

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