[Interaction between albumin-bound dinitrosyl iron complexes and reactive oxygen species].
It has been established that albumin-bound dinitrosyl iron complexes can be destroyed by superoxide radicals generated in a xanthine-xanthine oxidase system. It was shown that peroxynitrite also effectively destroyed albumin-bound dinitrosyl iron complexes. At the same time, hydrogen peroxide and tert-butyl hydroperoxide did not stimulate the destruction of albumin-bound dinitrosyl iron complexes up to concentrations one order higher than the content of NO. The data have been obtained indicating that dinitrosyl iron complexes possess the vasodilatory activity. It has been proposed that peroxynitrite and superoxide radical, by causing the destruction of albumin-bound dinitrosyl iron complexes, affect the physiological properties of nitric oxide.
Shumaev
K B
KB
Gubkin
A A
AA
Gubkina
S A
SA
Gudkov
L L
LL
Lakomkin
V L
VL
Topunov
A F
AF
Vanin
A F
AF
Ruuge
E K
EK
D000818:Animals; D001794:Blood Pressure / Q000187:drug effects; D007501:Iron / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D007700:Kinetics; D008297:Male; D009569:Nitric Oxide / Q000737:chemistry; D009589:Nitrogen Oxides / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D051381:Rats; D017208:Rats, Wistar; D017382:Reactive Oxygen Species / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000494:pharmacology
D009589:Nitrogen Oxides; D017382:Reactive Oxygen Species; D012710:Serum Albumin, Bovine; D009569:Nitric Oxide; C073661:dinitrosyl iron complex; D007501:Iron