Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Acidianus ambivalens | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
caldariellaquinol + O2 + n H+/in | Acidianus ambivalens | - |
caldariellaquinone + H2O + n H+/out | - |
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Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acidianus ambivalens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
caldariellaquinol + O2 + n H+/in | - |
Acidianus ambivalens | caldariellaquinone + H2O + n H+/out | - |
? | |
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 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
aa3 quinol oxidase | - |
Acidianus ambivalens |
aa3-type quinol oxidase | - |
Acidianus ambivalens |