Role of PhOH and Tyrosine in Selective Oxidation of Hydrocarbons

Abstract

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.

The Dual Function of PhOH Included in the Coordination Sphere of the Nickel Complexes in the Processes of Oxidation with Dioxygen

“…CO has been identified as an anti-apoptotic molecule in mammals. Recently, a human enzyme was found to regulate the activity of matrix metalloproteinase I (MMP-I), which is involved in tumor metastasis, by binding to the cytoplasmic transmembrane tail peptide MMP-I [ 16 , 17 ].…”

“…Similarly, the self-organization into supramolecular nanostructures observed in the case of model metal complexes of porphyrin with amino acids, tyrosine, and histidine can be considered as a regulatory factor influencing the oxygenation reactions of organic substances going through the mechanisms of action of Cytochrome P450-dependent monooxygenases [ 17 , 18 , 19 ].…”

“…This may be one of the reasons for the regulatory action of Tyr, which may reduce the activity of the Ni-ARD enzyme. The role of the second coordination sphere, including the Tyr fragment, and the participation of the Tyr fragment in the decrease in the enzyme activity is suggested, for example, in the action of Homoprotocatechuate 2,3-dioxygenase [ 17 ].…”

“…AFM SOLVER P47/SMENA/ was used with Silicon Cantilever NSG11S (NT MDT), which has curvature radius of 10 nm, or a 2-nm tip height, 10–15 µm, and a cone angle ≤ 22°. It was used in taping mode at a resonant frequency of 150 KHz [ 10 , 17 ]. A waterproof modified Silicon surface was used for the self-assembly growth due to H-bonding of Ni-contaning systems.…”

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

“…All structures are on various heights ranging from a minimum of 3-4 nm to a maximum of ~20-25 nm (in a form resembling three almost merged spheres). The structure of complex Ni2(AcO)3(acac)•MP•2H2O (Figure 4a) was defined by mass spectrometry, electron and IR spectroscopy, and element analysis [42]. It is known [3] that heteroligand complexes in reactions with electrophiles are characterized by higher activity compared to homoligand complexes.…”