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New Insights Into the L-Tryptophan Nitration Mechanism Catalyzed by the TxtE Cytochrome P450

Author

Listed:
  • Stéphanie Aguero

    (Équipe ECMO, Laboratoire de Biologie Tissulaire et d’Ingénierie (LBTI), UMR5305, Université Lyon 1, Lyon, France)

  • Simon Megy

    (Équipe ECMO, Laboratoire de Biologie Tissulaire et d’Ingénierie (LBTI), UMR5305, Université Lyon 1, Lyon, France)

  • Aurélie Thibaut

    (Protein Science Facility, SFR BioSciences, UAR3444/US8, 69367 Lyon, France)

  • Frédéric Delolme

    (Protein Science Facility, SFR BioSciences, UAR3444/US8, 69367 Lyon, France)

  • Virginie Gueguen Chaignon

    (Protein Science Facility, SFR BioSciences, UAR3444/US8, 69367 Lyon, France)

  • Raphaël Terreux

    (Équipe ECMO, Laboratoire de Biologie Tissulaire et d’Ingénierie (LBTI), UMR5305, Université Lyon 1, Lyon, France)

Abstract

Cytochromes P450 are multifunctional enzymes which usually act as mono-oxygenases. However, the CYP450 Thaxtomin E has been shown to carry out a direct nitration reaction on the aromatic residue L-Tryptophan. The details of the related mechanism by which TxtE generates ONOO° radicals through its ferric complex have been partially elucidated.

Suggested Citation

  • Stéphanie Aguero & Simon Megy & Aurélie Thibaut & Frédéric Delolme & Virginie Gueguen Chaignon & Raphaël Terreux, 2023. "New Insights Into the L-Tryptophan Nitration Mechanism Catalyzed by the TxtE Cytochrome P450," Biomedical Journal of Scientific & Technical Research, Biomedical Research Network+, LLC, vol. 48(3), pages 39761-39769, February.
    • Handle: RePEc:abf:journl:v:48:y:2023:i:3:p:39761-39769
    DOI: 10.26717/BJSTR.2023.48.007658
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