A new water-soluble bacterial NADH: fumarate oxidoreductase.
Klebsiella pneumoniae
cytoplasmic NADH:fumarate oxidoreductase
electron transport
fumarate respiration
Journal
FEMS microbiology letters
ISSN: 1574-6968
Titre abrégé: FEMS Microbiol Lett
Pays: England
ID NLM: 7705721
Informations de publication
Date de publication:
11 11 2020
11 11 2020
Historique:
received:
16
09
2020
accepted:
22
10
2020
pubmed:
28
10
2020
medline:
22
7
2021
entrez:
27
10
2020
Statut:
ppublish
Résumé
The cytoplasmic fumarate reductase of Klebsiella pneumoniae (FRD) is a monomeric protein which contains three prosthetic groups: noncovalently bound FMN and FAD plus a covalently bound FMN. In the present work, NADH is revealed to be an inherent electron donor for this enzyme. We found that the fumarate reductase activity of FRD significantly exceeds its NADH dehydrogenase activity. During the catalysis of NADH:fumarate oxidoreductase reaction, FRD turnover is limited by a very low rate (∼10/s) of electron transfer between the noncovalently and covalently bound FMN moieties. Induction of FRD synthesis in K. pneumoniae cells was observed only under anaerobic conditions in the presence of fumarate or malate. Enzymes with the FRD-like domain architecture are widely distributed among various bacteria and apparently comprise a new type of water-soluble NADH:fumarate oxidoreductases.
Identifiants
pubmed: 33107907
pii: 5941483
doi: 10.1093/femsle/fnaa175
pii:
doi:
Substances chimiques
Fumarates
0
Malates
0
Water
059QF0KO0R
NAD
0U46U6E8UK
malic acid
817L1N4CKP
NADH Dehydrogenase
EC 1.6.99.3
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of FEMS.