Literature summary for 7.1.1.7 extracted from

Korshunov, S.; Imlay, K.R.; Imlay, J.A.
The cytochrome bd oxidase of Escherichia coli prevents respiratory inhibition by endogenous and exogenous hydrogen sulfide (2016), Mol. Microbiol., 101, 62-77 .

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ABJ9 and P0ABK2 and P56100	P0ABJ9 i.e. subunit cydA, P0ABK2 i.e. subunit cydB, P56100 i.e. subunit cydX	-

General Information

General Information	Comment	Organism
physiological function	when cystine is provided and sulfide levels rise, Escherichia coli becomes strictly dependent upon cytochrome bd oxidase for continued respiration. Low-micromolar levels of sulfide inhibit the proton-pumping cytochrome bo oxidase. In the absence of the back-up cytochrome bd oxidase, growth fails. Exogenous sulfide elicits the same effect	Escherichia coli

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Release 2023.1 (January 2023)