Resolution of mitochondrial NADH dehydrogenase and isolation of two iron-sulfur proteins

Biochemistry. 1982 Feb 2;21(3):590-4. doi: 10.1021/bi00532a027.


The low molecular weight NADH dehydrogenase which can be solubilized from the mitochondrial NADH-ubiquinone oxidoreductase complex with chaotropic agents consists of three subunits in equimolar ratio [Galante, Y. M., & Hatefi, Y. (1979) Arch. Biochem. Biophys. 192, 559]. The largest subunit (subunit I) can be completely separated from the other two (subunits II + III) by treatment with sodium trichloroacetate and ammonium sulfate fractionation. Both the subunit I and subunit II + III fractions contain iron and acid-labile sulfur. From visible and EPR spectroscopy and the iron and acid-labile sulfide content, we propose that the subunit II + III fraction contains a binuclear cluster. The cluster structure present in subunit I is as yet unclear. On separation of the subunits of NADH dehydrogenase, the FMN is lost.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Cytochrome Reductases / isolation & purification*
  • Electron Spin Resonance Spectroscopy
  • Iron-Sulfur Proteins / isolation & purification*
  • Iron-Sulfur Proteins / metabolism
  • Kinetics
  • Macromolecular Substances
  • Metalloproteins / isolation & purification*
  • Mitochondria / enzymology*
  • NADH Dehydrogenase / isolation & purification*
  • NADH Dehydrogenase / metabolism
  • Spectrophotometry


  • Iron-Sulfur Proteins
  • Macromolecular Substances
  • Metalloproteins
  • Cytochrome Reductases
  • NADH Dehydrogenase