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Biochim Biophys Acta ; 1090(1): 133-8, 1991 Aug 27.
Article in English | MEDLINE | ID: mdl-1832016

ABSTRACT

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.


Subject(s)
Alcaligenes/genetics , NADH Dehydrogenase/genetics , Neurospora crassa/genetics , Quinone Reductases/genetics , Alcaligenes/enzymology , Amino Acid Sequence , Animals , Base Sequence , Binding Sites/genetics , Cattle , Flavin Mononucleotide/metabolism , Iron/metabolism , Mitochondria/enzymology , Molecular Sequence Data , NAD/metabolism , NAD(P)H Dehydrogenase (Quinone) , NADH Dehydrogenase/chemistry , Neurospora crassa/enzymology , Quinone Reductases/chemistry , Sequence Alignment , Sulfur/metabolism
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