Background: In Account, we show that the AFM method allows not only monitoring the morphological
changes of biological structures fixed on the surface due to H-bonds. The AFM method also makes it possible to study the
self-organization of metal complexes simulating the active center of enzymes due to intermolecular H-bonds into stable
nanostructures, the sizes of which are much smaller than the studied biological objects. The possible role of intermolecular hydrogen bonds in the formation of stable supramolecular metal complexes, which are effective catalysts for the oxidation of alkylarenes to hydro peroxides by molecular oxygen and mimic the selective active sites of enzymes, was first
studied by AFM.
Methods and results: The formation of supramolecular structures due tointermolecular hydrogen bonds and, possibly,
other non-covalent interactions,based on homogenous catalysts and models of active centers enzymes,heteroligand nickel
and iron complexes, was proven by AFM-technique. AFMstudies of supramolecular structures were carried out using
NSG30 cantileverwith a radius of curvature of 2 nm, in the tapping mode. To form nanostructureson the surface of a hydrophobic chemically modified silicon surface as asubstrate, the sample was prepared using a spin-cotting process from
solutionsof the nickel and iron complexes. The composition and the structure of thecomplex Ni2(acac)(OAc)3∙NMP∙2H2O
weredetermined in earlier works  using various methods: mass spectrometry, UV- andIR-spectroscopy, elemental analysis, polarography. Self-assembly of supramolecular structures isdue to intermolecular interactions with a certain coordination of theseinteractions, which may be a consequence of the properties of the componentsthemselves, the participation
of hydrogen bonds and other non-covalentinteractions, as well as the balance of the interaction of these componentswith
the surface. UsingAFM, approaches have been developed for fixing on the surface andquantifying parameters of cells.
Conclusion: This Account summarizes the authors' achievements in using the atomic force microscopy (AFM) method to
study, the role of intermolecular hydrogen bonds (and other non-covalent interactions) and supramolecular structures in
the mechanisms of catalysis. The obtained data of AFM based on nickel and iron complexes, which are effective catalysts
and models of active sites of enzymes, indicate a high probability of the formation of supramolecular structures in real
conditions of catalytic oxidation, and can bring us closer to understanding enzymes activity. With sensitive AFM method,
it is possible to observe the self-organization of model systems into stable nanostructures due to H-bonds and possibly
other non-covalent interactions, which can be considered as a step towards modeling the active sites of enzymes. Methodical approaches of atomic force microscopy for the study of morphological changes of cells have been developed.