Titelbild: A Cytochrome P450 TxtE Model System with Mechanistic and Theoretical Evidence for a Heme Peroxynitrite Active Species (Angew. Chem. 49/2024)

Tryptophan nitration chemistry of an economically impactful heme enzyme, TxtE, has been modeled utilizing synthetic heme mimics by Sam P. de Visser, Gayan B. Wijeratne et al. in their Research Article (e202409430). Therein, spectroscopic and theoretical characterizations strongly suggest the occurre...

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Veröffentlicht in:Angewandte Chemie 2024-12, Vol.136 (49), p.n/a
Hauptverfasser: Mondal, Pritam, Udukalage, Dhilanka, Mohamed, Abubaker A., Wong, Henrik P. H., Visser, Sam P., Wijeratne, Gayan B.
Format: Artikel
Sprache:eng
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Zusammenfassung:Tryptophan nitration chemistry of an economically impactful heme enzyme, TxtE, has been modeled utilizing synthetic heme mimics by Sam P. de Visser, Gayan B. Wijeratne et al. in their Research Article (e202409430). Therein, spectroscopic and theoretical characterizations strongly suggest the occurrence of a heme peroxynitrite active species, closely paralleling mechanistic propositions put forward for TxtE enzyme. Precise mechanistic details and key structure–activity relationships present important findings to be implemented in next generation therapeutic and synthetic applications.
ISSN:0044-8249
1521-3757
DOI:10.1002/ange.202419283