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Literature summary extracted from

  • Hiromoto, T.; Ataka, K.; Pilak, O.; Vogt, S.; Stagni, M.S.; Meyer-Klaucke, W.; Warkentin, E.; Thauer, R.K.; Shima, S.; Ermler, U.
    The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex (2009), FEBS Lett., 583, 585-590.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.12.99.6 overproduced in Escherichia coli BL21(DE3) cells Methanocaldococcus jannaschii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.12.99.6 mutant C176A crystallized in the presence of dithiothreitol, at 1.95 A resolution Methanocaldococcus jannaschii

Protein Variants

EC Number Protein Variants Comment Organism
1.12.99.6 C176A the Cys176 sulfur and unknown ligands of the iron complex of the wild-type enzyme are replaced by the dithiothreitol present in the crystallization solution Methanocaldococcus jannaschii

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.12.99.6 CO
-
 Methanocaldococcus jannaschii
1.12.99.6 cyanide
-
 Methanocaldococcus jannaschii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.12.99.6 Fe iron center octahedrally coordinated by one dithiothreitol-sulfur and one dithiothreitol-oxygen, two CO, the nitrogen of 2-pyridinol and the 6-formylmethyl group of 2-pyridinol in an acyliron ligation Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
1.12.99.6 Methanocaldococcus jannaschii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.12.99.6
-
 Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
1.12.99.6 [Fe]-hydrogenase
-
 Methanocaldococcus jannaschii

Cofactor

EC Number Cofactor Comment Organism Structure
1.12.99.6 additional information iron-guanylylpyridinol Methanocaldococcus jannaschii