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Literature summary extracted from

  • Siletsky, S.A.; Rappaport, F.; Poole, R.K.; Borisov, V.B.
    Evidence for fast electron transfer between the high-spin haems in cytochrome bd-I from Escherichia coli (2016), PLoS ONE, 11, e0155186 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.1.1.7
-
 Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.7 membrane
-
 Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.1.1.7 ubiquinol + O2 + H+[side 1] Escherichia coli
-
 ubiquinone + H2O + H+[side 2]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.7 Escherichia coli
-
-
-
7.1.1.7 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.7 ubiquinol + O2 + H+[side 1]
-
 Escherichia coli ubiquinone + H2O + H+[side 2]
-
 ?

Synonyms

EC Number Synonyms Comment Organism
7.1.1.7 cytochrome bd-I
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.7 heme the enzyme contains one low-spin haem (b558) and the two high-spin haems (b595 and d) as the redox-active cofactors Escherichia coli

General Information

EC Number General Information Comment Organism
7.1.1.7 physiological function the interheme electron backflow reaction induced by photodissociation of CO from heme d in one-electron reduced cytochrome bd-I comprises two kinetically different phases: the fast electron transfer from heme d to heme b595 within 0.2-1.5 micros and the slower electron equilibration with tau of about 16 micros. At 200 ns, there is no electron transfer Escherichia coli