Improved resolution of 3-mercaptopropionate dioxygenase active site provided by ENDOR spectroscopy offers insight into catalytic mechanism.
(1)H Mims ENDOR
DFT
Thiol dioxygenase
computational
hydrogen bonding
mononuclear non-heme iron
pulsed EPR spectroscopy
sulfur-oxidation
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
21 Feb 2024
21 Feb 2024
Historique:
received:
28
11
2023
revised:
13
02
2024
accepted:
15
02
2024
medline:
24
2
2024
pubmed:
24
2
2024
entrez:
23
2
2024
Statut:
aheadofprint
Résumé
3-mercaptopropionate (3MPA) dioxygenase (MDO) is a mononuclear non-heme iron enzyme that catalyzes the O
Identifiants
pubmed: 38395308
pii: S0021-9258(24)00153-4
doi: 10.1016/j.jbc.2024.105777
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
105777Informations de copyright
Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
CONFLICT OF INTEREST The authors declare that they have no conflicts of interest with the contents of this article.