Abstract
The large subunit HoxC of the H2-sensing [NiFe] hydrogenase from Ralstonia eutropha was purified without its small subunit. Two forms of HoxC were identified. Both forms contained iron but only substoichiometric amounts of nickel. One form was a homodimer of HoxC whereas the second also contained 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 Ni-Fe site provides direct evidence that Fe precedes Ni in the course of metal center assembly.
Original language | English (US) |
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Pages (from-to) | 4292-4296 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 579 |
Issue number | 20 |
DOIs | |
State | Published - Aug 15 2005 |
Externally published | Yes |
Keywords
- Maturation
- Metal center assembly
- Ralstonia eutropha
- [NiFe] hydrogenase
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology