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Literature summary for 1.12.7.2 extracted from

  • Forzi, L.; Koch, J.; Guss, A.M.; Radosevich, C.G.; Metcalf, W.W.; Hedderich, R.
    Assignment of the [4Fe-4S] clusters of Ech hydrogenase from Methanosarcina barkeri to individual subunits via the characterization of site-directed mutants (2005), FEBS J., 272, 4741-4753.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C42S mutant enzyme with almost no activity in the reaction with H2 and oxidized benzyl viologen Methanosarcina barkeri
C45S mutants with about 5% of the wild-type activity in the reaction with H2 and oxidized benzyl viologen Methanosarcina barkeri
C48S mutant enzyme with almost no activity in the reaction with H2 and oxidized benzyl viologen Methanosarcina barkeri
C73S mutants with about 5% of the wild-type activity in the reaction with H2 and oxidized benzyl viologen Methanosarcina barkeri
C76S mutant enzyme with almost no activity in the reaction with H2 and oxidized benzyl viologen Methanosarcina barkeri
C79S mutants with about 5% of the wild-type activity in the reaction with H2 and oxidized benzyl viologen Methanosarcina barkeri
C83S mutant enzyme with approximately 10% of the activity of the wild-type enzyme in the reaction with H2 and oxidized benzyl viologen Methanosarcina barkeri

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane bound to Methanosarcina barkeri 16020
-

Organism

Organism UniProt Comment Textmining
Methanosarcina barkeri
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methanosarcina barkeri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2 + ferredoxin + oxidized metronidazole
-
Methanosarcina barkeri H+ + ferredoxin + reduced metronidazole
-
?
H2 + oxidized benzyl viologen wild-type enzyme catalysed the reduction of benzylviologen at fourfold higher rates than the reduction of ferredoxin Methanosarcina barkeri reduced benzyl viologen + H+
-
?

Synonyms

Synonyms Comment Organism
Ech hydrogenase
-
Methanosarcina barkeri

Cofactor

Cofactor Comment Organism Structure
iron-sulfur centre the three [4Fe-4S] clusters simultaneously mediate electron and proton transfer and thus could be an essential part of the proton-translocating machinery Methanosarcina barkeri