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

Stéphanie Aguero, Simon Megy, Aurélie Thibaut, Frédéric Delolme, Virginie Gueguen Chaignon and Raphaël Terreux
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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

Biomedical Journal of Scientific & Technical Research, 2023, vol. 48, issue 3, 39761-39769

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.

Keywords: Journals on Medical Drug and Therapeutics; Journals on Emergency Medicine; Physical Medicine and Rehabilitation; Journals on Infectious Diseases Addiction Science and Clinical Pathology; Open Access Clinical and Medical Journal; Journals on Biomedical Science; List of Open Access Medical Journal; Journals on Biomedical Engineering; Open Access Medical Journal; Biomedical Science Articles; Journal of Scientific and Technical Research (search for similar items in EconPapers)
Date: 2023
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Persistent link: https://EconPapers.repec.org/RePEc:abf:journl:v:48:y:2023:i:3:p:39761-39769

DOI: 10.26717/BJSTR.2023.48.007658

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