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Nitration of Tyrosine and Tyrosyl Residues in Myoglobin under the Action of Visible Light in the Presence of Riboflavin and Nitrite
Abstract
Protein tyrosine nitration is considered as one of the types of post-translational modification of proteins, indicating disruptions in metabolic and signaling functions of nitric oxide •NO and development of oxidative nitrosative stress. We have considered the non-enzymatic pathway of protein nitration under the action of visible light in the presence of riboflavin and nitrite. Using mass spectrometry method, it is shown that redox processes photosensitized by riboflavin and involving nitrite and tyrosine/tyrosyl residues lead to nitration of tyrosyl residues Tyr-103 and Tyr-146 in polypeptide chain of horse heart myoglobin. Possible role of riboflavin and other natural photosensitizers in modification and damage of proteins in conditions when the body is exposed to intense visible light in the presence of nitrites in the blood is discussed.
About the Authors
I. I. Stepuro
Institute of Biochemistry of Biologically Active Compounds of the National Academy of Sciences of Belarus
Belarus
Belarus
Grodno
S. A. Ageiko
Institute of Biochemistry of Biologically Active Compounds of the National Academy of Sciences of Belarus
Belarus
Belarus
Grodno
V. I. Stsiapura
International Sakharov Environmental State Institute of Belarusian State University
Belarus
Belarus
Minsk
A. V. Yantsevich
Institute of Bioorganic Chemistry of the National Academy of Sciences of Belarus
Belarus
Belarus
Minsk
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Review
For citations:
Stepuro I.I., Ageiko S.A., Stsiapura V.I., Yantsevich A.V. Nitration of Tyrosine and Tyrosyl Residues in Myoglobin under the Action of Visible Light in the Presence of Riboflavin and Nitrite. Zhurnal Prikladnoii Spektroskopii. 2023;90(3):423-433. (In Russ.)
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