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
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

1365494

Informations 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.

Auteurs

Hafiz Saqib Ali (HS)

Chemistry Research Laboratory, Department of Chemistry and the INEOS Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, United Kingdom.

Sam P de Visser (SP)

Manchester Institute of Biotechnology and Department of Chemical Engineering, The University of Manchester, Manchester, United Kingdom.

Classifications MeSH