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 |
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Keywords
- [NiFe] hydrogenase
- Maturation
- Metal center assembly
- Ralstonia eutropha
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
A model system for [NiFe] hydrogenase maturation studies : Purification of an active site-containing hydrogenase large subunit without small subunit. / Winter, Gordon; Buhrke, Thorsten; Lenz, Oliver; Jones, Anne Katherine; Forgber, Michael; Friedrich, Bärbel.
In: FEBS Letters, Vol. 579, No. 20, 15.08.2005, p. 4292-4296.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A model system for [NiFe] hydrogenase maturation studies
T2 - Purification of an active site-containing hydrogenase large subunit without small subunit
AU - Winter, Gordon
AU - Buhrke, Thorsten
AU - Lenz, Oliver
AU - Jones, Anne Katherine
AU - Forgber, Michael
AU - Friedrich, Bärbel
PY - 2005/8/15
Y1 - 2005/8/15
N2 - 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.
AB - 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.
KW - [NiFe] hydrogenase
KW - Maturation
KW - Metal center assembly
KW - Ralstonia eutropha
UR - http://www.scopus.com/inward/record.url?scp=23644455994&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=23644455994&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2005.06.064
DO - 10.1016/j.febslet.2005.06.064
M3 - Article
C2 - 16061234
AN - SCOPUS:23644455994
VL - 579
SP - 4292
EP - 4296
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 20
ER -