Vanag V K, Kuznetsov A N
Biofizika. 1984 Jan-Feb;29(1):23-9.
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.
分析了酶活性中心和底物（S）的电子自旋均等于1/2的最简单酶促反应（ER）方案。结果表明，对于δg机制以及恒定磁场（MF）对电子自旋转换作用的弛豫机制，酶 - 底物复合物单重态和三重态之间的转换可用具有确定常数的单分子反应来描述。通过图解法得到了稳态ER速率对基本ER常数和单重态转换常数的依赖性。结果表明，在ER基本常数之间具有确定相关性的情况下，改变单重态转换常数的MF可影响ER速率。当[S]远小于Km（Km——米氏常数）时，所考虑的ER在动力学特征上符合自由基复合反应（RR），当[S]约大于Km时，MF对ER相对于RR的特定影响得以显现。在这些条件下，MF的作用相对于RR情况可显著增强，这取决于ER基本常数之间的相关性。
