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A Raman Spectroscopic Study of the Conformation of Flavin Adenine Dinucleotide, a CoEnzyme of D-Amino Acid Oxidase

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Abstract

The spectra of surface-enhanced Raman scattering of D-amino acid oxidase from pig kidney were recorded and analyzed using silver nanoparticles; characteristic spectral parameters of changes in the conformation of the flavinadenine dinucleotide cofactor during activation of the enzyme by D-amino acids were revealed. It was found that the time during which changes in the conformation of the flavinadenine dinucleotide were recorded depended on the substrate specificity of the enzyme: in the presence of D-alanine, this took several seconds, and in the presence of D-serine, minutes.

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REFERENCES

  1. L. Pollegioni and G. Molla, Cell Press 29 (6), 276 (2011).

    CAS  Google Scholar 

  2. K. Yagi, K. Okamura, et al., Biochim. Biophys. Acta 146, 77 (1967).

    Article  CAS  PubMed  Google Scholar 

  3. R. Upadhya, H. Nagajyothi, and S. G. Bhat, Process Biochem. 35, 7 (1999).

    Article  CAS  Google Scholar 

  4. L. Pollegioni, B. Langkau, and W. Tischer, J. Biol. Chem. 268 (19), 1385 (1993).

    Article  Google Scholar 

  5. L. Pollegioni, S. Sacchi, and G. Murtas, Front. Mol. Biosci. 5, 107 (2018).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  6. R. Konno, et al. Arch. Toxicol. 74, 473 (2000).

    Article  CAS  PubMed  Google Scholar 

  7. H. Wei, N. Gong, et al., Pharmacol. Biochem. Behav. 111, 30 (2013).

    Article  CAS  PubMed  Google Scholar 

  8. J. Sasabe, Y. Miyoshi, et al., Nat. Microbiol. 1 (10), 16125 (2016).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  9. A. L. Kalinichenko et al., Redox Biol. 60, 2213 (2023).

    Article  Google Scholar 

  10. S. Moussa, G. Murtas, et al., ACS Appl. Bio Mater. 4, 5598 (2021).

    Article  CAS  PubMed  Google Scholar 

  11. L. Rodriguez-Lorenzo, L. Fabris, and R. A. Alvarez-Puebla. Anal. Chim. Acta 745, 10 (2012).

    Article  CAS  PubMed  Google Scholar 

  12. A. A. Semenova, E. A. Goodilin, N. A. Brazhe, et al., J. Mater. Chem. 22, 24530 (2012).

    Article  CAS  Google Scholar 

  13. Y. Nishina, T. Kitagawa, and K. Shiga, J. Biochem. 84, 925 (1978).

    Article  CAS  PubMed  Google Scholar 

  14. T. Kitagawa, Y. Nishina, et al., Biochemistry 18, 1804 (1979).

    Article  CAS  PubMed  Google Scholar 

  15. Y. Nishina, H. Tojo, and K. Shiga, J. Biochem. 104, 227 (1988).

    Article  CAS  PubMed  Google Scholar 

  16. Y. Nishina, R. Miura, and H. Tojo, J. Biochem. 99, 329 (1986).

    Article  CAS  PubMed  Google Scholar 

  17. Y. Nishina, K. Shiga, et al., J. Biochem. 88, 411 (1980).

    Article  CAS  PubMed  Google Scholar 

  18. Y. Nishina, K. Shiga, and R. Miura, J. Biochem. 94, 1979 (1983).

    Article  CAS  PubMed  Google Scholar 

  19. https://www.uniprot.org/uniprotkb/P14920/entry.

  20. M. Gabler, M. Hensel, and L. Fischer, Enzyme Microb. Technol. 27 (8), 605 (2000).

    Article  CAS  PubMed  Google Scholar 

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Funding

The research was carried out with the financial support of the Russian Science Foundation, project no. 23-74-00006 for Zh. V. Bochkova and N. A. Brazhe, as well as the Interdisciplinary Scientific and Educational School of Moscow State University Molecular technologies of living systems and synthetic biology.

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Correspondence to G. V. Maksimov.

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Translated by E. Puchkov

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Abbreviations: DAAO, D-amino acid oxidase; FAD, flavin adenine dinucleotide; RS, Raman spectroscopy; SERS, surface-enhanced Raman scattering.

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Bochkova, J.V., Liu, W., Brazhe, N.A. et al. A Raman Spectroscopic Study of the Conformation of Flavin Adenine Dinucleotide, a CoEnzyme of D-Amino Acid Oxidase. BIOPHYSICS 68, 719–724 (2023). https://doi.org/10.1134/S0006350923050068

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  • DOI: https://doi.org/10.1134/S0006350923050068

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