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Eur J Biochem. 1994 Mar 1;220(2):551-8.

Disruption of the gene encoding the NADH-binding subunit of NADH: ubiquinone oxidoreductase in Neurospora crassa. Formation of a partially assembled enzyme without FMN and the iron-sulphur cluster N-3.

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Institut für Biochemie, Heinrich-Heine-Universität Düsseldorf, Germany.


In this study, the gene of the 51-kDa NADH-binding subunit of the mitochondrial NADH:ubiquinone oxidoreductase (complex I) in Neurospora crassa was inactivated by homologous replacement with a defective gene copy. The resulting mutant, nuo51, lacks the 51-kDa subunit and shows no complex I activity but still grows at one third of the wild-type growth rate. The enzyme activity of the alternative NADH:ubiquinone oxidoreductase(s) is increased twofold while the activities of the other mitochondrial respiratory enzymes are normal. Complex I is almost completely assembled except for the NADH-binding subunit and still possesses three out of the four EPR-detectable iron-sulphur clusters. Since the deleted subunit contains the sequence motif for one tetranuclear iron-sulphur cluster, the missing cluster N-3 is considered to be bound to this subunit.

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