Catalytic divergencies in the mechanism of L-arginine hydroxylating nonheme iron enzymes.
QM/MM
cluster models
dioxygenases
enzyme catalysis
inorganic reaction mechanisms
iron enzymes
Journal
Frontiers in chemistry
ISSN: 2296-2646
Titre abrégé: Front Chem
Pays: Switzerland
ID NLM: 101627988
Informations de publication
Date de publication:
2024
2024
Historique:
received:
04
01
2024
accepted:
22
01
2024
medline:
26
2
2024
pubmed:
26
2
2024
entrez:
26
2
2024
Statut:
epublish
Résumé
Many enzymes in nature utilize a free arginine (L-Arg) amino acid to initiate the biosynthesis of natural products. Examples include nitric oxide synthases, which generate NO from L-Arg for blood pressure control, and various arginine hydroxylases involved in antibiotic biosynthesis. Among the groups of arginine hydroxylases, several enzymes utilize a nonheme iron(II) active site and let L-Arg react with dioxygen and
Identifiants
pubmed: 38406558
doi: 10.3389/fchem.2024.1365494
pii: 1365494
pmc: PMC10884159
doi:
Types de publication
Journal Article
Review
Langues
eng
Pagination
1365494Informations de copyright
Copyright © 2024 Ali and de Visser.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. The author(s) declare that they were an editorial board member of Frontiers, at the time of submission. This had no impact on the peer review process and the final decision.