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Literature summary extracted from

  • Guiral, M.; Tron, P.; Aubert, C.; Gloter, A.; Iobbi-Nivol, C.; Giudici-Orticoni, M.T.
    A membrane-bound multienzyme, hydrogen-oxidizing, and sulfur-reducing complex from the hyperthermophilic bacterium Aquifex aeolicus (2005), J. Biol. Chem., 280, 42004-42015.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.12.98.4 NADPH presence of NADPH increases the sulfur reduction activity, but NADPH alone cannot be used as electron donor Aquifex aeolicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.12.98.4 cytoplasm location of catalytic subunit Aquifex aeolicus 5737
-
1.12.98.4 membrane location of subunit C Aquifex aeolicus 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.12.98.4 Iron sequence is predicted to carry four [4Fe-4S] clusters Aquifex aeolicus

Organism

EC Number Organism UniProt Comment Textmining
1.12.98.4 Aquifex aeolicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.12.98.4 purification of enzyme by solubilísation with sodium deoxycholate, in presence of ACA and glycerol Aquifex aeolicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.12.98.4 additional information no substrate: dimethyl sulfoxide, thiosulfate. Presence of NADPH increases the sulfur reducing activity. Hydrogenase reaction ond sulfur reduction by enzyme are energetically coupled but take place in two separate complexes. Electron transfer is mediated by quinones Aquifex aeolicus ?
-
 ?
1.12.98.4 polysulfide + H2
-
 Aquifex aeolicus H2S
-
 ?
1.12.98.4 S + H2
-
 Aquifex aeolicus H2S
-
 ?
1.12.98.4 tetrathionate + H2
-
 Aquifex aeolicus ? + H+
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.12.98.4 molybdopterin
-
 Aquifex aeolicus