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Literature summary for 1.12.99.6 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
Search for more literature for 1.12.99.6

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Clostridium acetobutylicum

Protein Variants

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

Inhibitors

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

Organism

Organism UniProt Comment Textmining
Clostridium acetobutylicum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Clostridium acetobutylicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2 + acceptor
-
 Clostridium acetobutylicum H2-acceptor
-
 r
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

Synonyms Comment Organism
hydA
-
 Clostridium acetobutylicum
[FeFe]-hydrogenase
-
 Clostridium acetobutylicum

pH Optimum

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

Cofactor

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