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Effect of Dinitrosyl Iron Complex on Albumin Conformation

Elvin S. Allakhverdiev1,2,a*, Georgy V. Maksimov1,3,b*, Oleg V. Rodnenkov2, Oksana G. Luneva1, Georgy V. Tsoraev1, Aleksey D. Ivanov3, Alexander I. Yusipovich1, and Tamila V. Martynyuk2

1Faculty of Biology, Lomonosov Moscow State University, 119991 Moscow, Russia

2Russian National Medical Research Center of Cardiology, 121552 Moscow, Russia

3Federal State Autonomous Educational Institution of Higher Education “National Research Technological University “MISIS”, 119049 Moscow, Russia

* To whom correspondence should be addressed.

Received February 8, 2021; Revised March 12, 2021; Accepted March 22, 2021
Binding of dinitrosyl iron complex (DNIC) to albumin was studied using time-resolved fluorescence (TRF) and electron spin resonance (ESR) spectroscopy. It was found that the fluorescence lifetime of bovine serum albumin (BSA) and human serum albumin (HSA) decreases with binding and depends on DNIC concentration. The observed biexponential pattern of the BSA tryptophan (Trp) fluorescence decay is explained by the presence of two tryptophan residues in the protein molecule. We believe that DNIC forms stable complexes with the cysteine (Cys34) residue in the domain I of albumin. It was shown that the lifetime of albumin tryptophan fluorescence decreased during co-incubation of BSA with DNICs and glutathione. Effects of DNIC on the binding of specific spin-labeled fatty acids with albumin in human blood plasma were studied in vitro. The presence of DNIC in blood plasma does not change conformation of albumin domains II and III. We suggest that the most possible interaction between DNICs and albumin is the formation of a complex; and nitrosylation of the cysteine residue in the albumin domain I occurs without the changes in albumin conformation.
KEY WORDS: albumin, dinitrosyl iron complex, electron spin resonance, nitrogen oxide, time-resolved fluorescence

DOI: 10.1134/S0006297921050023