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Literature summary for 1.12.99.6 extracted from

  • Fritsch, J.; Scheerer, P.; Frielingsdorf, S.; Kroschinsky, S.; Friedrich, B.; Lenz, O.; Spahn, C.
    The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre (2011), Nature, 479, 249-253.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
to 1.5 A resolution. The heterodimeric enzyme consists of a large subunit harbouring the catalytic centre in the H2-reduced state and a small subunit containing an electron relay consisting of three different iron-sulfur clusters. The cluster proximal to the active site displays an unprecedented [4Fe-3S] structure and is coordinated by six cysteines. According to the current model, this cofactor operates as an electronic switch depending on the nature of the gas molecule approaching the active site. It serves as an electron acceptor in the course of H2 oxidation and as an electron-delivering device upon O2 attack at the active site Cupriavidus necator

Organism

Organism UniProt Comment Textmining
Cupriavidus necator P31891
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Cupriavidus necator DSM 428 P31891
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Synonyms

Synonyms Comment Organism
HoxG
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Cupriavidus necator

Cofactor

Cofactor Comment Organism Structure
iron-sulfur centre data from crystal structure Cupriavidus necator