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Literature summary for 1.12.7.2 extracted from

  • Nakos, G.; Mortenson, L.E.
    Structural properties of hydrogenase from Clostridium pasteurianum W5 (1971), Biochemistry, 10, 2442-2449.
    View publication on PubMed
Search for more literature for 1.12.7.2

General Stability

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

Inhibitors

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

Molecular Weight [Da]

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

Organism

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

Substrates and Products (Substrate)

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

Subunits

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