Literature summary 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.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.12.99.6	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

EC Number	Organism	UniProt	Comment	Textmining
1.12.99.6	Cupriavidus necator	P31891	-	-
1.12.99.6	Cupriavidus necator DSM 428	P31891	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
1.12.99.6	HoxG	-	Cupriavidus necator

Cofactor

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

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Release 2023.1 (January 2023)