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Literature summary for 1.12.98.2 extracted from

  • Lyon, E.J.; Shima, S.; Boecher, R.; Thauer, R.K.; Grevels, F.W.; Bill, E.; Roseboom, W.; Albracht, S.P.J.
    Carbon monoxide as an intrinsic ligand to iron in the active site of the iron-sulfur-cluster-free hydrogenase H2-forming methylenetetrahydromethanopterin dehydrogenase as revealed by infrared spectroscopy (2004), J. Am. Chem. Soc., 126, 14239-14248.
    View publication on PubMed
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General Stability

General Stability Organism
enzyme and cofactor are light sensitive Methanothermobacter marburgensis

Inhibitors

Inhibitors Comment Organism Structure
CN- reversible Methanothermobacter marburgensis
CO reversible Methanothermobacter marburgensis

Metals/Ions

Metals/Ions Comment Organism Structure
Iron enzyme contains iron bound to an mercaptoethanol-extractable cofactor of unknown structure, contains intrinsic CO bound to iron Methanothermobacter marburgensis
additional information no iron-sulfur-cluster Methanothermobacter marburgensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
 x * 38000 Methanothermobacter marburgensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5,10-methenyltetrahydromethanopterin + H2 Methanothermobacter marburgensis involved in methanogenesis 5,10-methylenetetrahydromethanopterin + H+
-
 r

Organism

Organism UniProt Comment Textmining
Methanothermobacter marburgensis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Methanothermobacter marburgensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methenyltetrahydromethanopterin + H2 involved in methanogenesis Methanothermobacter marburgensis 5,10-methylenetetrahydromethanopterin + H+
-
 r
5,10-methenyltetrahydromethanopterin + H2 reverse reaction under argon atmosphere Methanothermobacter marburgensis 5,10-methylenetetrahydromethanopterin + H+
-
 r
additional information no reduction of viologen dyes in the presence of H2 Methanothermobacter marburgensis ?
-
 ?

Subunits

Subunits Comment Organism
? x * 38000 Methanothermobacter marburgensis

Cofactor

Cofactor Comment Organism Structure
additional information enzyme contains iron bound to a mercaptoethanol-extractable cofactor of unknown structure, contains intrinsic CO bound to iron Methanothermobacter marburgensis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.01
-
 CO pH 6.0, 40°C, under N2 Methanothermobacter marburgensis
0.1
-
 CN- pH 6.0, 40°C, under N2 Methanothermobacter marburgensis