The air-inactivation of formate dehydrogenase FdsDABG from Cupriavidus necator.
FdsDABG
Formate dehydrogenase
Steady-state kinetics
Superoxide
Superoxide dismutase
Xanthine oxidase
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:
06 2022
06 2022
Historique:
received:
23
11
2021
revised:
28
02
2022
accepted:
06
03
2022
pubmed:
22
3
2022
medline:
14
4
2022
entrez:
21
3
2022
Statut:
ppublish
Résumé
The nature of air-inactivation of the formate dehydrogenase FdsDABG from Cupriavidus necator has been investigated. It is found that superoxide, generated in the reaction of reduced enzyme with oxygen, is responsible for the loss of activity and that superoxide dismutase protects the enzyme from air-inactivation. Inhibition appears to be due to the reaction of superoxide with the catalytically essential MoS group of the enzyme's molybdenum center in such a way that generates sulfite. SYNOPSIS: Superoxide generated in the reaction of reduced formate dehydrogenase FdsDABG from Cupriavidus necator with O
Identifiants
pubmed: 35313132
pii: S0162-0134(22)00077-0
doi: 10.1016/j.jinorgbio.2022.111788
pii:
doi:
Substances chimiques
Superoxides
11062-77-4
Superoxide Dismutase
EC 1.15.1.1
Formate Dehydrogenases
EC 1.17.1.9
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
111788Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.