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

• Type: Article in International Scientific Journal
• Date: 1991

Authors

preis, d (Author) Other; weidner, u (Author) Other; conzen, c (Author) Other; azevedo, je (Author) ICBAS; nehls, u (Author) Other; rohlen, d (Author) Other; van der pas, j (Author) Other; sackmann, u (Author) Other; schneider, r (Author) Other; werner, s (Author) Other; weiss, h (Author) Other

Journal

Title: Biochimica et Biophysica Acta - Gene Structure and Expression

Vol. 1090

Pages: 133-138

ISSN: 0167-4781

Publisher: Elsevier B.V.

Indexing

ISI Web of Knowledge

Scopus - 20 Citations

Scientific classification

FOS: Natural sciences

Other information

Authenticus ID: P-007-5AM

DOI: 10.1016/0167-4781(91)90049-R

Abstract (EN): 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.

Language: English

Type (Professor's evaluation): Scientific