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Literature summary for 1.12.99.6 extracted from

  • Adams, M.W.W.
    The mechanisms of hydrogen activation and carbon monoxide binding by hydrogenase I and hydrogenase II of Clostridium pasteurianum (1987), J. Biol. Chem., 262, 15054-15061.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
CO binds irreversibly, hydrogenase I has a lower affinity for CO than hydrogenase II Clostridium pasteurianum

Metals/Ions

Metals/Ions Comment Organism Structure
Fe iron-sulfur cluster as well as 4Fe-4S-ferredoxin-type cluster Clostridium pasteurianum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
H2 + acceptor Clostridium pasteurianum 2 different enzymes, hydrogenase I and II H+ + reduced acceptor
-
 r

Organism

Organism UniProt Comment Textmining
Clostridium pasteurianum
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-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Clostridium pasteurianum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2 + acceptor 2 different enzymes, hydrogenase I and II Clostridium pasteurianum H+ + reduced acceptor
-
 r
H2 + acceptor methyl viologen acts as electron acceptor Clostridium pasteurianum H+ + reduced acceptor
-
 r

Synonyms

Synonyms Comment Organism
hydrogenase I (bidirectional) catalyzes H2 oxidation and reduction at similar rates Clostridium pasteurianum
hydrogenase II (uptake) preferentially catalyzes H2 oxidation Clostridium pasteurianum