Literature summary for 1.12.99.6 extracted from

Winter, G.; Buhrke, T.; Lenz, O.; Jones, A.K.; Forgber, M.; Friedrich, B.
A model system for [NiFe] hydrogenase maturation studies: Purification of an active site-containing hydrogenase large subunit without small subunit (2005), FEBS Lett., 579, 4292-4296.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe	the large subunit HoxC is purified without its small subunit. Two forms of HoxC are identified. Both forms contain iron but only substoichiometric amounts of nickel. One form is a homodimer of HoxC whereas the second also contains the NiFe site maturation proteins HypC and HypB. Despite the presence of the NiFe active site in some of the proteins, both forms, which lack the FeS clusters normally present in hydrogenases, cannot activate hydrogen. The incomplete insertion of nickel into the NiFe site provides direct evidence that Fe precedes Ni in the course of metal center assembly	Cupriavidus necator

Organism

Organism	UniProt	Comment	Textmining
Cupriavidus necator	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
the large subunit HoxC is purified without its small subunit. Two forms of HoxC are identified. Both forms contain iron but only substoichiometric amounts of nickel. One form is a homodimer of HoxC whereas the second also contains the Ni-Fe site maturation proteins HypC and HypB. Despite the presence of the Ni-Fe active site in some of the proteins, both forms, which lack the Fe-S clusters normally present in hydrogenases, cannot activate hydrogen. The incomplete insertion of nickel into the NiFe site provides direct evidence that Fe precedes Ni in the course of metal center assembly	Cupriavidus necator

Purification (Comment)

Organism

the large subunit HoxC is purified without its small subunit. Two forms of HoxC are identified. Both forms contain iron but only substoichiometric amounts of nickel. One form is a homodimer of HoxC whereas the second also contains the Ni-Fe site maturation proteins HypC and HypB. Despite the presence of the Ni-Fe active site in some of the proteins, both forms, which lack the Fe-S clusters normally present in hydrogenases, cannot activate hydrogen. The incomplete insertion of nickel into the NiFe site provides direct evidence that Fe precedes Ni in the course of metal center assembly

Cupriavidus necator

Synonyms

Synonyms	Comment	Organism
H2-sensing [NiFe] hydrogenase	-	Cupriavidus necator