E. coli cytochrome bd-I requires Asp58 in the CydB subunit for catalytic activity.
FEBS Lett
; 596(18): 2418-2424, 2022 09.
Article
en En
| MEDLINE
| ID: mdl-36029102
The reduction of oxygen to water is crucial to life and a central metabolic process. To fulfil this task, prokaryotes use among other enzymes cytochrome bd oxidases (Cyt bds) that also play an important role in bacterial virulence and antibiotic resistance. To fight microbial infections by pathogens, an in-depth understanding of the enzyme mechanism is required. Here, we combine bioinformatics, mutagenesis, enzyme kinetics and FTIR spectroscopy to demonstrate that proton delivery to the active site contributes to the rate limiting steps in Cyt bd-I and involves Asp58 of subunit CydB. Our findings reveal a previously unknown catalytic function of subunit CydB in the reaction of Cyt bd-I.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas de Escherichia coli
/
Escherichia coli
Idioma:
En
Revista:
FEBS Lett
Año:
2022
Tipo del documento:
Article
País de afiliación:
Alemania
Pais de publicación:
Reino Unido