Literature summary for 7.1.1.4 extracted from

Muller, F.H.; Bandeiras, T.M.; Urich, T.; Teixeira, M.; Gomes, C.M.; Kletzin, A.
Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate:quinone oxidoreductase (2004), Mol. Microbiol., 53, 1147-1160.

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Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Acidianus ambivalens	P94117 and P94118	P94117 (doxB, catalytic core), P94118 (doxC)	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
caldariella quinol + O2 + n H+/in	-	Acidianus ambivalens	caldariella quinone + H2O + n H+/out	-	?

Subunits

Subunits	Comment	Organism
?	the doxD and doxA genes form a bicistronic operon in the Acidianus ambivalens genome, physically separated from the doxBCEF operon encoding the catalytic and the other subunits of the terminal quinol:oxygen oxidoreductase. Subunits with apparent molecular masses of 56000 Da (DoxB) and 61000 Da (DoxC) appear in the preparation of the terminal oxidase. Both enzymes 1. thiosulfate dehydrogenase (quinone) (EC 1.8.5.2, composed of the subunits DoxA and DoxD) and 2. caldariella quinol:dioxygen oxidoreductase (composed of the major subunits DoxB and DoxC and the minor subunit DoxE) form separate entities. The thiosulfate dehydrogenase (quinone) and the terminal oxidase might still form a loose aggregation in the membrane, transferring electrons rapidly either directly via the bound caldariella quinol molecule or indirectly via free caldariella quinol	Acidianus ambivalens

Synonyms

Synonyms	Comment	Organism
caldariella quinol:dioxygen oxidoreductase	-	Acidianus ambivalens
cytochrome aa3	-	Acidianus ambivalens
terminal quinol:oxygen oxidoreductase	-	Acidianus ambivalens

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Release 2023.1 (January 2023)