[Kinetic analysis of the possible effect of a constant magnetic field on the rate of enzymatic reactions].

The simplest scheme of enzymatic reaction (ER) in which the electronic spins of the enzymatic active centre and substrate (S) equal 1/2 is analysed. It is shown that for delta g-mechanism, as well as for the relaxation mechanism of the action of constant magnetic field (MF) on the electronic spin conversion the conversions between singlet and triplet states of the enzyme-substrate complex can be described by monomolecular reactions with definite constants. The dependence of the rate of steady-state ER upon elementary ER constants and upon singlet conversion constants is obtained by the graph method. It is shown that MF changing the singlet conversion constants can influence the rate of ER under definite correlation between elementary constant of ER. In the case of [S] much less than Km (Km--Michaelis constant) the considered ER is in accordance with the recombination reaction of free radicals (RR) by kinetic characteristics, when [S] approximately greater than Km the specific influence of MF on ER with respect to RR is displayed. Under these conditions the action of MF can grow significantly with respect to RR case depending on the correlation between the elementary constants of ER.