Formation of a new type of dinitrosyl iron complexes bound to cysteine modified with methylglyoxal |
| |
Authors: | K. B. Shumaev S. A. Gubkina A. F. Vanin D. Sh. Burbaev V. P. Mokh A. F. Topunov E. K. Ruuge |
| |
Affiliation: | 17643. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071, Russia 27643. Russian Cardiology Research and Production Center, Moscow, 121552, Russia 37643. Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow, 119334, Russia 47643. Physical Faculty, Moscow State University, Moscow, 119991, Russia
|
| |
Abstract: | It has been shown that interaction of cysteine dinitrosyl iron complexes with methylglyoxal leads to the formation of a new type of dinitrosyl iron complexes, EPR spectrum of these complexes essentially differs from spectra of dinitrosyl iron complexes containing unmodified thiol. The products of the cysteine reaction with methylglyoxal are hemithioacetals, Schiff bases and thiazolidines, which most likely serve as ligands for the new type of dinitrosyl iron complexes. It has been shown that the new type of dinitrosyl iron complexes as cysteine dinitrosyl iron complexes, which are physiological donors of nitric oxide, exert a vasodilator effect. It has also been found that the oxidative destruction of the new type of dinitrosyl iron complexes occurs at normal oxygen partial pressure, but these dinitrosyl iron complexes remain rather stable under hypoxia modeling. An assumption that the destruction of the new type of dinitrosyl iron complexes is caused by the formation of a bound peroxynitrite-containing intermediate is made. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|