PMID:15922336
| Citation |
Velazquez, I, Nakamaru-Ogiso, E, Yano, T, Ohnishi, T and Yagi, T (2005) Amino acid residues associated with cluster N3 in the NuoF subunit of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli. FEBS Lett. 579:3164-8 |
|---|---|
| Abstract |
The NuoF subunit, which harbors NADH-binding site, of Escherichia coli NADH-quinone oxidoreductase (NDH-1) contains five conserved cysteine residues, four of which are predicted to ligate cluster N3. To determine this coordination, we overexpressed and purified the NuoF subunit and NuoF+E subcomplex in E. coli. We detected two distinct EPR spectra, arising from a [4Fe-4S] cluster (g(x,y,z)=1.90, 1.95, and 2.05) in NuoF, and a [2Fe-2S] cluster (g(x,y,z)=1.92, 1.95, and 2.01) in NuoE subunit. These clusters were assigned to clusters N3 and N1a, respectively. Based on the site-directed mutagenesis experiments, we identified that cluster N3 is ligated to the 351Cx2Cx2Cx40C398 motif. |
| Links |
PubMed Online version:10.1016/j.febslet.2005.05.005 |
| Keywords |
Amino Acids/metabolism; Electron Spin Resonance Spectroscopy; Electron Transport; Escherichia coli/enzymology; Escherichia coli Proteins/genetics; Escherichia coli Proteins/isolation & purification; Escherichia coli Proteins/metabolism; Iron/pharmacology; Protein Subunits/chemistry; Protein Subunits/genetics; Protein Subunits/isolation & purification; Protein Subunits/metabolism; Protons; Quinone Reductases/chemistry; Quinone Reductases/genetics; Quinone Reductases/isolation & purification; Quinone Reductases/metabolism; Sulfur/pharmacology |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.
