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Nitration of Tyrosine and Tyrosyl Residues in Myoglobin by the Action of Visible Light in the Presence of Riboflavin and Nitrite**

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Journal of Applied Spectroscopy Aims and scope

The nitration of tyrosyl residues in proteins is considered a type of post-translational modification of proteins, indicating disruptions in the metabolic and signaling functions of nitric oxide •NO and the development of oxidative nitrosative stress. We have examined the nonenzymatic pathway of protein nitration by the action of visible light in the presence of riboflavin and nitrite. Mass spectrometry was used to show that riboflavin-photosensitized redox processes involving nitrite and tyrosine or tyrosyl residues lead to nitration of residues Tyr-103 and Tyr-146 in the polypeptide chain of horse heart myoglobin. A possible role is discussed for riboflavin and other natural photosensitizers in the modification and damage of proteins when the body is exposed to intense visible light in the presence of nitrites in the blood.

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Authors and Affiliations

  1. Institute of Biochemistry and Biologically Active Compounds of the National Academy of Sciences of Belarus, Grodno, Belarus

    I. I. Stepuro & S. A. Ageiko

  2. International Sakharov Environmental State Institute of Belarusian State University, Minsk, Belarus

    V. I. Stsiapura

  3. Institute of Bioorganic Chemistry of the National Academy of Sciences of Belarus, Minsk, Belarus

    A. V. Yantsevich

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  1. I. I. Stepuro
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  2. S. A. Ageiko
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  3. V. I. Stsiapura
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  4. A. V. Yantsevich
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Correspondence to V. I. Stsiapura.

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**Presented at the Second International Seminar on Molecular Spectroscopy and the Photochemistry of Macroheterocyclic Compounds, October 18–19, 2022, Minsk, Belarus.

Translated from Zhurnal Prikladnoi Spektroskopii, Vol. 90, No. 3, pp. 423–433, May–June, 2023.

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Stepuro, I.I., Ageiko, S.A., Stsiapura, V.I. et al. Nitration of Tyrosine and Tyrosyl Residues in Myoglobin by the Action of Visible Light in the Presence of Riboflavin and Nitrite**. J Appl Spectrosc 90, 543–553 (2023). https://doi.org/10.1007/s10812-023-01565-z

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  • DOI: https://doi.org/10.1007/s10812-023-01565-z

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