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Literature summary extracted from

  • Hambourger, M.; Gervaldo, M.; Svedruzic, D.; King, P.W.; Gust, D.; Ghirardi, M.; Moore, A.L.; Moore, T.A.
    [FeFe]-hydrogenase-catalyzed H2 production in a photoelectrochemical biofuel cell (2008), J. Am. Chem. Soc., 130, 2015-2022.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.12.99.6 expressed in Escherichia coli Clostridium acetobutylicum

Protein Variants

EC Number Protein Variants Comment Organism
1.12.99.6 energy production use in photochemical energy conversion systems Clostridium acetobutylicum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.12.99.6 O2 competitive inhibitor, irreversible inhibition Clostridium acetobutylicum

Organism

EC Number Organism UniProt Comment Textmining
1.12.99.6 Clostridium acetobutylicum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.12.99.6
-
 Clostridium acetobutylicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.12.99.6 H2 + acceptor
-
 Clostridium acetobutylicum H2-acceptor
-
 r
1.12.99.6 H2 + oxidized electron acceptor both platinum and pyrolytic graphite edge/HydA electrodes are effective catalysts operating near the reversible potential of the H+/H2 redox couple Clostridium acetobutylicum H+ + reduced electron acceptor
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.12.99.6 hydA
-
 Clostridium acetobutylicum
1.12.99.6 [FeFe]-hydrogenase
-
 Clostridium acetobutylicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.12.99.6 7
-
 optimal catalytic activity near neutral pH Clostridium acetobutylicum

Cofactor

EC Number Cofactor Comment Organism Structure
1.12.99.6 iron-sulfur centre contains one [2Fe-2S] and three [4Fe-4S] clusters Clostridium acetobutylicum