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. 1971 Dec;68(12):3242–3246. doi: 10.1073/pnas.68.12.3242

In Vitro Formation of Assimilatory Reduced Nicotinamide Adenine Dinucleotide Phosphate: Nitrate Reductase from a Neurospora Mutant and a Component of Molybdenum-Enzymes

Alvin Nason 1, Kuo-Yung Lee 1, Su-Shu Pan 1, Paul A Ketchum 1,*, Antonio Lamberti 1, James DeVries 1
PMCID: PMC389631  PMID: 4399835

Abstract

An active Neurospora-like assimilatory NADPH-nitrate reductase (EC 1.6.6.2), which can be formed in vitro by incubation of extracts of nitrate-induced Neurospora crassa mutant nit-1 with extracts of (a) certain other nonallelic nitrate reductase mutants, (b) uninduced wild type, or (c) xanthine oxidizing and liver aldehyde-oxidase systems was also formed by combination of the nit-1 extract with other acid-treated enzymes known to contain molybdenum. These molybdenum enzymes included (a) nitrogenase, or its molybdenum-iron protein, from Clostridium, Azotobacter, and soybeannodule bacteroids, (b) bovine liver sulfite oxidase, (c) respiratory formate-nitrate reductase from Escherichia coli, (d) NADH-nitrate reductase from foxtail grass (Setaria faberii), and (e) FADH2- and reduced methyl viologennitrate reductase preparations from certain Neurospora mutants. Several molybdenum-amino-acid complexes, as possible catalytic models of nitrogenase, were inactive (as were some previously tested 20 nonmolybdenum enzymes) in place of the acid-treated molybdenum-containing enzymes. The results imply the existence of a molybdenum-containing component shared by the known molybdenum-enzymes.

Keywords: nitrogenases, sulfite oxidase, E. coli

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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