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Literature summary for 1.12.99.6 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)

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

Crystallization (Commentary)

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

Protein Variants

Protein Variants Comment Organism
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

Inhibitors Comment Organism Structure
CO
-
Methanocaldococcus jannaschii
cyanide
-
Methanocaldococcus jannaschii

Metals/Ions

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methanocaldococcus jannaschii

Synonyms

Synonyms Comment Organism
[Fe]-hydrogenase
-
Methanocaldococcus jannaschii

Cofactor

Cofactor Comment Organism Structure
additional information iron-guanylylpyridinol Methanocaldococcus jannaschii