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Literature summary for 1.12.98.4 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

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

Localization

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
polysulfide + H2
-
Aquifex aeolicus H2S
-
?
S + H2
-
Aquifex aeolicus H2S
-
?
tetrathionate + H2
-
Aquifex aeolicus ? + H+
-
?

Cofactor

Cofactor Comment Organism Structure
molybdopterin
-
Aquifex aeolicus