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Literature summary extracted from

  • Nakos, G.; Mortenson, L.E.
    Structural properties of hydrogenase from Clostridium pasteurianum W5 (1971), Biochemistry, 10, 2442-2449.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.12.7.2 after treatment with 4 mM urea, 100% activity after several hours Clostridium pasteurianum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.12.7.2 Sodium mersalyl at 12.2 mol per mol protein, 70% inhibition Clostridium pasteurianum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.12.7.2 30000
-
 2 * 30000, hydrogenase I, SDS-PAGE Clostridium pasteurianum
1.12.7.2 60000
-
 gel filtration, hydrogenase I Clostridium pasteurianum

Organism

EC Number Organism UniProt Comment Textmining
1.12.7.2 Clostridium pasteurianum
-
-
-
1.12.7.2 Clostridium pasteurianum
-
 hydrogenase I, bidirectional hydrogenase
-
1.12.7.2 Clostridium pasteurianum W5
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.12.7.2 H2 + electron acceptor methylene blue as electron acceptor Clostridium pasteurianum H+ + reduced electron acceptor
-
 ?
1.12.7.2 H2 + electron acceptor methyl viologen as electron acceptor Clostridium pasteurianum H+ + reduced electron acceptor
-
 ?
1.12.7.2 H2 + electron acceptor methylene blue as electron acceptor Clostridium pasteurianum W5 H+ + reduced electron acceptor
-
 ?
1.12.7.2 H2 + electron acceptor methyl viologen as electron acceptor Clostridium pasteurianum W5 H+ + reduced electron acceptor
-
 ?

Subunits

EC Number Subunits Comment Organism
1.12.7.2 dimer 2 * 30000, hydrogenase I, SDS-PAGE Clostridium pasteurianum