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Literature summary for 7.1.1.7 extracted from

  • Borisov, V.B.; Forte, E.; Siletsky, S.A.; Sarti, P.; Giuffre, A.
    Cytochrome bd from Escherichia coli catalyzes peroxynitrite decomposition (2015), Biochim. Biophys. Acta, 1847, 182-188 .
    View publication on PubMed
Search for more literature for 7.1.1.7

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli GO105/pTK1 cells Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
peroxynitrite addition of ONOO- to cytochrome bd in turnover with ascorbate and N,N,N',N'-tetramethyl-p-phenylenediamine causes the irreversible inhibition of about 15% of the enzyme fraction, due to the NO radical generated from ONOO-. Addition of ONOO- to cells expressing cytochrome bd as the only terminal oxidase, causes about 5% irreversible inhibition of O2 consumption. Purified cytochrome bd in turnover with O2 is able to metabolize ONOO- with an apparent turnover rate as high as about 10 mol ONOO- per mol of enzyme and per s at 25°C Escherichia coli

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information purified cytochrome bd in turnover with O2 is able to metabolize ONOO- with an apparent turnover rate as high as about 10 mol ONOO- per mol of enzyme and per s at 25°C Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
cytochrome bd
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
heme
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function the enzyme contributes to bacterial resistance to nitric oxide and hydrogen peroxide Escherichia coli