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    Biochim Biophys Acta. 1991 Aug 27;1090(1):133-8.

    Primary structures of two subunits of NADH: ubiquinone reductase from Neurospora crassa concerned with NADH-oxidation. Relationship to a soluble NAD-reducing hydrogenase of Alcaligenes eutrophus.

    Preis D, Weidner U, Conzen C, Azevedo JE, Nehls U, Röhlen D, van der Pas J, Sackmann U, Schneider R, Werner S, et al.

    Institut für Biochemie, Heinrich-Heine-Universität Düsseldorf, F.R.G.

    The primary structures of the nuclear-encoded 51 kDa and 78 kDa subunits of the respiratory chain NADH: ubiquinone reductase (complex I) from Neurospora crassa mitochondria were determined by sequencing cDNA and the N-terminus of the mature proteins. Both subunits are related to the soluble NAD-reducing hydrogenase of the bacterium Alcaligenes eutrophus. Sequence comparison between these subunits, the corresponding subunits of the bovine complex I and the bacterial NAD-reducing hydrogenase further confirms the binding sites of NAD(H), FMN and three iron-sulfur clusters.

    PMID: 1832016 [PubMed - indexed for MEDLINE]

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