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Literature summary for 1.12.99.6 extracted from

  • Shima, S.; Pilak, O.; Vogt, S.; Schick, M.; Stagni, M.S.; Meyer-Klaucke, W.; Warkentin, E.; Thauer, R.K.; Ermler, U.
    The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site (2008), Science, 321, 572-575.
    View publication on PubMed
Search for more literature for 1.12.99.6

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with an iron guanylyl pyridone, Methanocaldococcus jannaschii

Protein Variants

Protein Variants Comment Organism
C250A reduced activity Methanocaldococcus jannaschii

Inhibitors

Inhibitors Comment Organism Structure
CO CO is a competitive inhibitor with respect to H2 Methanocaldococcus jannaschii
O2 the enzyme is irreversibly inhibited under aerobic conditions Methanocaldococcus jannaschii

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2 + methenyltetrahydromethanopterin the heterolytic cleavage of H2 by the enzyme is dependent on the presence of methenyltetrahydromethanopterin Methanocaldococcus jannaschii H+ + methylenetetrahydromethanopterin
-
 r

Synonyms

Synonyms Comment Organism
[Fe]-hydrogenase
-
 Methanocaldococcus jannaschii

Cofactor

Cofactor Comment Organism Structure
iron-sulfur centre contains a mononuclear iron coordinated by the sulfur of cysteine 176, the iron center is the catalytically active constituent of an iron guanylyl pyridone cofactor Methanocaldococcus jannaschii