Effect of Dinitrosyl Iron Complex on Albumin Conformation

Allakhverdiev, Elvin S.; Максимов, Г. В.; Rodnenkov, O. V.; Luneva, O. G.; Tsoraev, Georgy V.; Ivanov, Aleksey D; Yusipovich, A. I.; Martynyuk, T V

doi:10.1134/s0006297921050023

Cited by 1 publication

(2 citation statements)

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“…Mammalian serum albumin is the major protein in blood plasma, as well as a vital component of lymph, interstitial, and cerebrospinal fluids [33,34]. This protein is responsible for colloidal-osmotic (oncotic) plasma pressure, as well as for the binding and transport of low-molecular-weight compounds: fatty acids, carotenoids, heme, and metal ions [34][35][36]. Albumin is ROS-modified under oxidative stress, e.g., under ischemia/reperfusion conditions [34,[36][37][38][39], and ischemically modified albumin contains the damaged metal-binding centers.…”

Section: Introductionmentioning

confidence: 99%

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Histidine-Bound Dinitrosyl Iron Complexes: Antioxidant and Antiradical Properties

Shumaev,

Kosmachevskaya,

Nasybullina

et al. 2023

IJMS

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Dinitrosyl iron complexes (DNICs) are important physiological derivatives of nitric oxide. These complexes have a wide range of biological activities, with antioxidant and antiradical ones being of particular interest and importance. We studied the interaction between DNICs associated with the dipeptide L-carnosine or serum albumin and prooxidants under conditions mimicking oxidative stress. The ligands of these DNICs were histidine residues of carnosine or His39 and Cys34 in bovine serum albumin. Carnosine-bound DNICs reduced the level of piperazine free radicals in the reaction system containing tert-butyl hydroperoxide (t-BOOH), bivalent iron ions, a nitroxyl anion donor (Angeli’s salt), and HEPES buffer. The ability of carnosine DNICs to intercept organic free radicals produced from t-BOOH decay could lead to this effect. In addition, carnosine DNICs reacted with the superoxide anion radical (O2•−) formed in the xanthine/xanthine oxidase enzymatic system. They also reduced the oxoferryl form of the heme group formed in the reaction of myoglobin with t-BOOH. DNICs associated with serum albumin were found to be rapidly destroyed in a model system containing metmyoglobin and t-BOOH. At the same time, these protein DNICs inhibited the t-BOOH-induced oxidative degradation of coenzymes Q9 and Q10 in rat myocardial homogenate. The possible mechanisms of the antioxidant and antiradical action of the DNICs studied and their role in the metabolism of reactive oxygen and nitrogen species are discussed.

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Section: Introductionmentioning

confidence: 99%

“…Two types of DNICs can be associated with human and bovine serum albumins. In the first type, iron is coordinated with a Cys34 residue and a low-molecular-weight thiol, e.g., glutathione [15,35,41]. In the second type, the non-protein thiol ligand is replaced with the histidine residue of the albumin protein chain [6,41].…”

Section: Introductionmentioning

confidence: 99%