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Literature summary extracted from

  • Lauterbach, L.; Liu, J.; Horch, M.; Hummel, P.; Schwarze, A.; Haumann, M.; Vincent, K.; Lenz, O.; Zebger, I.
    The hydrogenase subcomplex of the NAD+-reducing [NiFe] hydrogenase from Ralstonia eutropha - Insights into catalysis and redox interconversions (2011), Eur. J. Inorg. Chem., 2011, 1067-1079.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.12.1.2 FMN H2 oxidation by subunits HoxHY is enhanced on addition of excess FMN Cupriavidus necator

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.12.1.2 expression in Cupriavidus necator Cupriavidus necator

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.12.1.2 O2 incubation of subunits HoxHY with O2 at high potentials causes slow inactivation, but activity is recovered within seconds at potentials below -170 mV at 30°C, even in the presence of 2% O2; incubation of subunits HoxHY with O2 at high potentials causes slow inactivation, but activity is recovered within seconds at potentials below -170 mV at 30°C, even in the presence of 2% O2 Cupriavidus necator

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.12.1.2 Iron the active site iron atom has a standard ligation, i.e., one CO and two cyanide ligands Cupriavidus necator

Organism

EC Number Organism UniProt Comment Textmining
1.12.1.2 Cupriavidus necator P22319 subunit delta
-
1.12.1.2 Cupriavidus necator P22320 subunit beta
-
1.12.1.2 Cupriavidus necator DSM 428 P22319 subunit delta
-
1.12.1.2 Cupriavidus necator DSM 428 P22320 subunit beta
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.12.1.2 recombinant protein. The as-isolated module HoxHY is initially catalytically inactive, but after reductive activation at low potentials, exhibits both H2 oxidation and H+ reduction Cupriavidus necator

Synonyms

EC Number Synonyms Comment Organism
1.12.1.2 HoxH
-
 Cupriavidus necator
1.12.1.2 HoxS
-
 Cupriavidus necator

Cofactor

EC Number Cofactor Comment Organism Structure
1.12.1.2 4Fe-4S-center presence of a 4Fe-4S-center in addition to the active site iron Cupriavidus necator
1.12.1.2 FMN cofactor and stabilization of the active site Cupriavidus necator