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Amino acid residues associated with cluster n3 in the nuof subunit of the proton-translocating nadh-quinone oxidoreductase from escherichia coli

Academic Article
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Overview

authors

  • Velazquez, I.
  • Nakamaru-Ogiso, E.
  • Yano, T.
  • Ohnishi, T.
  • Yagi, Takao

publication date

  • June 2005

journal

  • FEBS Letters  Journal

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.

subject areas

  • Amino Acids
  • Electron Spin Resonance Spectroscopy
  • Electron Transport
  • Escherichia coli
  • Escherichia coli Proteins
  • Iron
  • Protein Subunits
  • Protons
  • Quinone Reductases
  • Sulfur
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Research

keywords

  • Escherichia coli
  • NADH-quinone oxidoreductase
  • NuoF
  • complex 1
  • electron paramagnetic resonance
  • iron-sulfur cluster
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Identity

International Standard Serial Number (ISSN)

  • 0014-5793

Digital Object Identifier (DOI)

  • 10.1016/j.febslet.2005.05.005

PubMed ID

  • 15922336
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Additional Document Info

start page

  • 3164

end page

  • 3168

volume

  • 579

issue

  • 14

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