Features of the decomposition of cationic nitrosyl iron complexes with N-ethylthiourea and penicillamine ligands in the presence of albumin

Autor: T. N. Rudneva, Natalia A. Sanina, Alexandra Yu. Kormukhina, Konstantin A. Lyssenko, Alexander I. Kotelnikov, O. V. Pokidova
Rok vydání: 2021
Předmět:
Zdroj: Inorganica Chimica Acta. 524:120453
ISSN: 0020-1693
DOI: 10.1016/j.ica.2021.120453
Popis: In this work, transformations of two cationic dinitrosyl iron complexes (DNICs), namely, mononuclear with N-ethylthiourea ligands [Fe(SC(NH2)(NHC2H5))2(NO)2]+Cl−∙[Fe(SC(NH2)(NHC2H5))Cl(NO)2]0 (complex 1) and binuclear with penicillamine ligands [Fe2(S(C(CH3)2CH(NH3)COOH))2(NO)4]SO4·5H2O (complex 2) have been investigated in an aqueous solution in the presence of bovine serum albumin (BSA) under anaerobic and aerobic conditions. The spectroscopic measurements have shown that the complexes bind to the protein, which leads to their stabilization. The resulting products are much more stable in the absence of oxygen. The fluorescence measurements indicated that complexes 1 and 2 interact with BSA with equilibrium constants K = 4.9∙105 M−1 and 5.3∙105 M−1, respectively. Complex 1 can bind to the surface due to weak intermolecular interactions, resulting in prolonged generation of NO. Also, the decay product of complex 1, both under anaerobic conditions and in the presence of oxygen, is coordinated with Cys34 and His39 in the hydrophobic pocket of albumin, as evidenced by the appearance of a shoulder at 370–410 nm. As a result of these interactions, a high molecular weight albumin-bound complex is formed, which then slowly decomposes in more than 40 h. Complex 2 and its products are adsorbed on the surface of the protein. However, in the presence of oxygen, protein does not significantly affect the NO release rate.
Databáze: OpenAIRE
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