The terminal oxidase cytochrome bd-I confers carbon monoxide resistance to Escherichia coli cells.
Carbon monoxide
Cytochrome
Heme protein
Inhibition
Resistance
Terminal 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:
10 2023
10 2023
Historique:
received:
12
04
2023
revised:
12
07
2023
accepted:
22
07
2023
medline:
21
8
2023
pubmed:
30
7
2023
entrez:
29
7
2023
Statut:
ppublish
Résumé
Carbon monoxide (CO) plays a multifaceted role in the physiology of organisms, from poison to signaling molecule. Heme proteins, including terminal oxidases, are plausible CO targets. Three quinol oxidases terminate the branched aerobic respiratory chain of Escherichia coli. These are the heme‑copper cytochrome bo
Identifiants
pubmed: 37515940
pii: S0162-0134(23)00223-4
doi: 10.1016/j.jinorgbio.2023.112341
pii:
doi:
Substances chimiques
Carbon Monoxide
7U1EE4V452
Copper
789U1901C5
Escherichia coli Proteins
0
Cytochrome b Group
0
Electron Transport Chain Complex Proteins
0
Cytochromes
0
Oxidoreductases
EC 1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
112341Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.