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
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

111788

Informations de copyright

Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.

Auteurs

Sheron Hakopian (S)

Department of Biochemistry, University of California, Riverside, Riverside, CA 92521, USA.

Dimitri Niks (D)

Department of Biochemistry, University of California, Riverside, Riverside, CA 92521, USA.

Russ Hille (R)

Department of Biochemistry, University of California, Riverside, Riverside, CA 92521, USA. Electronic address: russ.hille@ucr.edu.

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Classifications MeSH