The article analyzes the role of hydrogen bonds and supramolecular structures in enzyme catalysis and model systems. Hydrogen bonds play a crucial role in many enzymatic reactions. However, scientists have only recently attempted to harness the power of hydrogen bonds in homogeneous catalytic systems. One of the newest directions is associated with attempts to control the properties of catalysts by influencing the “second coordination sphere” of metal complexes. The role H-bonding, and the building of stable supramolecular nanostructures due to intermolecular H-bonds, based on catalytic active heteroligand iron (Fe) or nickel (Ni) complexes formed during hydrocarbon oxidations were assessed via the AFM (Atomic-force microscopy) method, which was proposed and applied by authors of this manuscript. Th is article also discusses the roles of hydrogen bonds and supramolecular structures in oxidation reactions catalyzed by heteroligand Ni and Fe complexes, which are not only effective homogeneous catalysts but also structural and functional models of Oxygenases.

For the first time AFM (atomic-force microscopy) was used to record significant changes in the geometric parameters of the image of erythrocytes in vitro under conditions of glycolytic starvation (ATP (Adenosine triphosphate) deficiency). The difference in the action of antioxidants, phenosan K, and Ihfan-10 on erythrocytes that we detected with AFM seems to be mainly due to their difference in hydrophobicity. We used the AFM method to research the self-organization of the components of the active center of P450 (Porphyrin-450) metalloenzymes that are part of a class of hemoproteins with functions of affinity to molecular oxygen O₂. Stable supramolecular nanostructures in the form of triangular prisms based on the iron porphyrin complex with amino acids due to self-assembly involving intermolecular hydrogen bonds were received. A possible scheme for the formation of such structures is proposed.

Earlier, we established that nickel or iron heteroligand complexes, which include PhOH (nickel complexes) or tyrosine residue (nickel or iron complexes), are not only hydrocarbon oxidation catalysts (in the case of PhOH), but also simulate the active centers of enzymes (PhOH, tyrosine). The AFM method established the self-organization of nickel or iron heteroligand complexes, which included tyrosine residue or PhOH, into supramolecular structures on a modified silicon surface. Supramolecular structures were formed as a result of H-bonds and other non-covalent intermolecular interactions and, to a certain extent, reflected the structures involved in the mechanisms of reactions of homogeneous and enzymatic catalysis. Using the AFM method, we obtained evidence at the model level in favor of the involvement of the tyrosine fragment as one of the possible regulatory factors in the functioning of Ni(Fe)ARD dioxygenases or monooxygenases of the family of cytochrome P450. The principles of actions of these oxygenases were used to create highly efficient catalytic systems for the oxidation of hydrocarbons.

Background: Stress factors lead to a shift in the antioxidant-prooxidant relationship, allowing an increase in the generation of reactive oxygen species (ROS) by mitochondria, which results in the development of oxidative stress. Consequently, it is possible to put forward an as-sumption that drugs which reduce the excessive generation of ROS by these organelles should in-crease the body's resistance to stress factors. Antioxidants can be used as such drugs. In this regard, the aim of this work was to study the bioenergetics characteristic of mitochondria under stress con-ditions and under the action of 2-ethyl-6-methyl-3-hydroxypyridinium hydroxybutanedioate (eth-oxidol). Methods: The antiradical activity of the drug was evaluated by the chemiluminescent method (CL). The functional state of the mitochondria was studied with reference to the level of lipid peroxida-tion by the spectrofluorimetry and in terms of fatty acid composition of mitochondrial membranes using the chromatography technique. The study of mitochondrial morphology was performed em-ploying the method of atomic force microscopy. Results: The injection in mice of ethoxidol at a dose of 10-5 mol/kg for 7 days led to the prevention of the stress-induced increase in the intensity of LPO in the membranes of the mitochondria, and swelling of these organelles; it also prevented a decrease in the content of unsaturated fatty acids, containing 18 and 20 carbon atoms. At the same time, ethoxidol increased the life expectancy of mice by 3.0-4.2 times in conditions of various types of hypoxia. Conclusion: The adaptogenic properties of ethoxidol can be attributed to its antiradical and antiox-idant properties.

It is known that the presence of redox-inactive metals in the active center of an enzyme has a significant effect on its activity. In this regard and for other reasons, the effect of redox-inactive metals on redox processes, such as electron transfer, oxygen and hydrogen atom transfer, as well as the breaking and formation of O–O bonds in reactions catalyzed by transition metals, has been widely studied. Many questions about the role of redox-inactive metals in the mechanisms of these reactions remain open. In this paper, the mechanism of catalysis by bi- and triple hetero-binuclear heteroligand complexes including Ni and redox-inactive alkali metals ((A) {Ni(acac)₂∙L²} and (B) {Ni(acac)₂∙L²∙PhOH} (L² = MSt (M = Li, Na, or K)) in the process of the selective oxidation of ethylbenzene by molecular oxygen into α-phenyl ethyl hydroperoxide is considered. The activity of A and B complexes towards O₂, ROOH, and RO₂^• radicals was studied. Based on kinetic data, we suggest that the high catalytic efficiency of B triple complexes in oxidation processes may be associated with the role of outer-sphere regulatory interactions, with the formation of stable supramolecular structures due to intermolecular H bonds. This assumption was confirmed using the AFM method. Prospects for studying catalysis by complexes ({Ni(acac)₂∙L²} and {Ni(acac)₂∙L²∙PhOH}) that are models of NiARD (Ni-Acyreductone dioxygenase) are discussed.