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Literature summary for 7.1.1.4 extracted from

  • Das, T.K.; Gomes, C.M.; Teixeira, M.; Rousseau, D.L.
    Redox-linked transient deprotonation at the binuclear site in the aa(3)-type quinol oxidase from Acidianus ambivalens: implications for proton translocation (1999), Proc. Natl. Acad. Sci. USA, 96, 9591-9596.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.1.1.4

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
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 Acidianus ambivalens 16020
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
caldariellaquinol + O2 + n H+/in Acidianus ambivalens
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 caldariellaquinone + H2O + n H+/out
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 ?

Organism

Organism UniProt Comment Textmining
Acidianus ambivalens
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
caldariellaquinol + O2 + n H+/in
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 Acidianus ambivalens caldariellaquinone + H2O + n H+/out
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 ?
caldariellaquinol + O2 + n H+/in the major quinone in aerobically grown Acidianus ambivalens is caldariellaquinone, which is a thiophenobenzoquinone present in the Sulfolobales. The detergent-solubilized enzyme oxidizes caldariellaquinol at a high rate and with high specificity. The heme a3 formyl group undergoes a redox-induced change in its hydrogen bonding, at a much faster rate in the membrane-integrated than in the purified enzyme. It is proposed that a functional role of the bound quinone, in addition to being involved in the electron transfer chain, is to facilitate the conformational changes in the enzyme required for its proper function. In addition, the nature of the redox-linked changes is studied in relation to the physiological conditions of Acidianus ambivalens, and a redox/proton translocation coupling site near the heme a3 formyl group is postulated Acidianus ambivalens caldariellaquinone + H2O + n H+/out
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 ?

Synonyms

Synonyms Comment Organism
aa3 quinol oxidase
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 Acidianus ambivalens
aa3-type quinol oxidase
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 Acidianus ambivalens