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Literature summary for 2.8.4.1 extracted from

  • Signor, L.; Knuppe, C.; Hug, R.; Schweizer, B.; Pfaltz, A.; Jaun, B.
    Methane formation by reaction of a methyl thioether with a photo-excited nickel thiolate-a process mimicking methanogenesis in archaea (2000), Chem. Eur. J., 6, 3508-3516.
    View publication on PubMed
Search for more literature for 2.8.4.1

Metals/Ions

Metals/Ions Comment Organism Structure
Ni(2+)
-
 Methanobacterium sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
methyl coenzyme M + coenzyme B Methanobacterium sp. key enzyme in methane formation by methanogenic Archaea methane + CoM-S-S-CoB
-
 ?

Organism

Organism UniProt Comment Textmining
Methanobacterium sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methyl coenzyme M + coenzyme B key enzyme in methane formation by methanogenic Archaea Methanobacterium sp. methane + CoM-S-S-CoB
-
 ?
additional information several bifunctional substrates tested, substrates contain both an aliphatic thiol and a methyl thioether function Methanobacterium sp. ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
F-430
-
 Methanobacterium sp.
additional information enzyme consists of 2 symmetry-equivalent active sites containing one molecule of the hydroporphinoid nickel complex coenzyme F-430, enzyme is active only if the metal center of coenzyme F-430 is in the nickel(I) form Methanobacterium sp.