The case for an oxidopyrylium intermediate in the mechanism of quercetin dioxygenases.
Dioxygenation
ESIPT
Flavonol
Oxidopyrylium
Photochemistry
Quercetin dioxygenase
Journal
Journal of inorganic biochemistry
ISSN: 1873-3344
Titre abrégé: J Inorg Biochem
Pays: United States
ID NLM: 7905788
Informations de publication
Date de publication:
10 2023
10 2023
Historique:
received:
30
03
2023
revised:
22
06
2023
accepted:
25
07
2023
medline:
21
8
2023
pubmed:
8
8
2023
entrez:
7
8
2023
Statut:
ppublish
Résumé
The quercetin dioxygenases (QDOs) are unusual metalloenzymes in that they display ring-opening dioxygenase activity with several different first-row transition metal ions which do not undergo redox changes during turnover. The QDOs are also unique in that the substrate binds as an η
Identifiants
pubmed: 37549474
pii: S0162-0134(23)00225-8
doi: 10.1016/j.jinorgbio.2023.112343
pii:
doi:
Substances chimiques
Dioxygenases
EC 1.13.11.-
Quercetin
9IKM0I5T1E
Flavonols
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
112343Informations de copyright
Copyright © 2023 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Patrick Farmer reports financial support and equipment, drugs, or supplies were provided by Baylor University.