The Role H-Bonding and Supramolecular Structures in Homogeneous and Enzymatic Catalysis

Int J Mol Sci. 2023 Nov 28;24(23):16874. doi: 10.3390/ijms242316874.

Abstract

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.

Keywords: AFM method; H-bonding; catalysis; models of Oxygenases; supramolecular structures.

MeSH terms

  • Catalysis
  • Coordination Complexes* / chemistry
  • Iron* / chemistry
  • Nickel / chemistry
  • Oxidation-Reduction
  • Oxygenases

Substances

  • Iron
  • Coordination Complexes
  • Oxygenases
  • Nickel

Grants and funding

This manuscript received budget funding from the Ministry of Education and Science of the Russian Federation within the framework of state funding of Emanuel NM Institute of Biochemical Physics RAS (project No. 122041300210-2) (“Physic-chemical foundations and principles of functioning of biological macromolecules, supramolecular systems of varying degrees of complexity, new research methods, use in modern high technologies”). Our AFM study of model complexes also received financial support from the Presidium of the Russian Academy of Sciences RAS 14P, State Register Number: AAAA-A17-1117121920169-0.