Abstract
This review examines the changes in the activity of plant, fungal, and bacterial enzymes from the oxidoreductase class - peroxidase, laccase, and veratric acid O-demethylase - that occurred under the influence of a series of high and very high dilutions of their low-molecular effectors, mainly of phenolic origin. A common feature of these observations is the demonstration of oscillatory changes in the activity of the studied enzymes, fluctuating between maximum and minimum values during incubation with progressive dilution of their effectors. The course of these oscillations is unique to the enzyme complex and the degree of effector dilution. It provides practical information regarding changes in the allosteric affinity of the enzyme-effector system. In addition to changes in activity, adaptation of the enzyme to a progressive series of effector dilutions was manifested by morphological differentiation of bacterial cells and increased production of the enzyme protein in dilutions with maximum activity or its disappearance at minimum activity. The presented review of experimental studies indicates that the biological information contained in successive iterations of a series of diluted effector changes according to the dilution rate. It affects all metabolic pathways of the organisms studied. The reproducibility of the obtained results was ensured by the use of a unified system for preparing dynamic effector dilutions in aqueous or alcoholic solutions.