ЗАЩИТНОЕ ДЕЙСТВИЕ ДИНИТРОЗИЛЬНЫХ КОМПЛЕКСОВ ЖЕЛЕЗА НА ГЕМОГЛОБИН ПРИ ОКИСЛИТЕЛЬНОЙ МОДИФИКАЦИИ ПЕРОКСИНИТРИТОМ
https://doi.org/10.20914/2304-4691-2020-3-369-371
Об авторах
Э. И. НасыбуллинаРоссия
О. В. Космачевская
Россия
К. Б. Шумаев
Россия
А. Ф. Топунов
Россия
Список литературы
1. Tsai M. et al.. Dinitrosyl Iron Complexes (DNICs): From Biomimetic Synthesis and Spectroscopic Characterization toward Unveiling the Biological and Catalytic Roles of DNICs. // Acc. Chem. Res. 2015. 48. 4. 1184-1193.
2. Hsiao H.Y., et al.. Fe in biosynthesis, translocation, and signal transduction of NO: toward bioinorganic engineering of dinitrosyl iron complexes into NO-delivery scaffolds for tissue engineering. // Dalton Trans. 2019 Apr 16.
3. Vanin A.F. Dinitrosyl iron complexes with thiol-containing ligands as a «working form» of endogenous nitric oxide. // Nitric Oxide. 2016. 54. 15-29.
4. Vanin A.F. Dinitrosyl iron complexes as a "working form" of nitric oxide in living. / Cambridge Scholars Publishing. 2019. 265 P.
5. Shumaev K.B., et al. Interaction of reactive oxygen and nitrogen species with albumin - and hemoglobin bound dinitrosyl iron complexes. // Nitric Oxide. 2008. 18. 37-46.
6. Shumaev K.B., et al. Dinitrosyl iron complexes bound with haemoglobin as markers of oxidative stress. // Methods in Enzymology. 2008. 436. 445-461.
7. Шумаев К.Б., et al. Взаимодействие оксоферрилмиоглобина и динитрозильных комплексов железа. // Биохимия. 2004. 69. 5. 699-705.
8. Shumaev K.B., et al. Protective effect of dinitrosyl iron complexes with glutathione in red blood cell lysis induced by hypochlorous acid. // Oxidative Medicine and Cellular Longevity. 2019. V. 2019, ArticleID2798154, 12 pages.
9. Pietraforte D., et al.Peroxynitrite-dependentmodifications of tyrosine residues in hemoglobin. Formation of tyrosyl radical(s) and 3 nitrotyrosine. // Amino Acids. 2003. 25. 3-4. 341-350.
10. Romero N., et al. Reaction of Human Hemoglobin with Peroxynitrite. // J. Biol. Chem. 2003. 278. 45. 44049-44057.
11. Herold S., et al. Kinetics of the reactions of nitrogen monoxide and nitrite with ferryl hemoglobin. // Free Rad. Biol. Med. 2003. 34. 531-545.
12. Vlasova I.I. Peroxidase activity of human hemoproteins: keeping the fire under control. // Molecules. 2018. 23. 2561.
13. Ford E., et al. Kinetics of the reactions of nitrogen dioxide with glutathione, cysteine, and uric acid at physiological pH. // Free Radic. Biol. Med. 32. 2002. 1314-1323.
14. Pietraforte D., Minetti M. One-electronoxidation pathway of peroxynitrite decomposition in human blood plasma: evidence for the formation of protein tryptophan-centredradicals. // Biochem J. 1997. 321. 734-750.
15. Alvarez B., et al. Peroxynitrite-dependenttryptophan nitration. // Chem Res Toxicol. 1996. 9. 2. 390-396.
Рецензия
Для цитирования:
Насыбуллина Э.И., Космачевская О.В., Шумаев К.Б., Топунов А.Ф. ЗАЩИТНОЕ ДЕЙСТВИЕ ДИНИТРОЗИЛЬНЫХ КОМПЛЕКСОВ ЖЕЛЕЗА НА ГЕМОГЛОБИН ПРИ ОКИСЛИТЕЛЬНОЙ МОДИФИКАЦИИ ПЕРОКСИНИТРИТОМ. Актуальная биотехнология. 2020;(3):369-371. https://doi.org/10.20914/2304-4691-2020-3-369-371