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 |
|---|---|
| Pages (from-to) | 4292-4296 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 579 |
| Issue number | 20 |
| DOIs | |
| Publication status | Published - Aug 15 2005 |
Keywords
- Maturation
- Metal center assembly
- Ralstonia eutropha
- [NiFe] hydrogenase
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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Winter, G., Buhrke, T., Lenz, O., Jones, A. K., Forgber, M., & Friedrich, B. (2005). A model system for [NiFe] hydrogenase maturation studies: Purification of an active site-containing hydrogenase large subunit without small subunit. FEBS Letters, 579(20), 4292-4296. https://doi.org/10.1016/j.febslet.2005.06.064