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PMID: 4399835 Published · ppublish English Journal Article

Invitro formation of assimilatory reduced nicotinamide adenine dinucleotide phosphate: nitrate reductase from a Neurospora mutant and a component of molybdenum-enzymes.

Nason A, Lee KY, Pan SS, Ketchum PA, Lamberti A, DeVries J

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) FADH(2)- 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.

MeSH Terms
Animals Azotobacter/enzymology Cattle Clostridium/enzymology Escherichia coli/enzymology Flavin-Adenine Dinucleotide In Vitro Techniques Iron Liver/enzymology Molybdenum Mutation NADP Neurospora/enzymology Neurospora crassa/enzymology Oxidoreductases Poaceae/enzymology Soybeans/enzymology Sulfites Xanthines
Chemicals
Sulfites Xanthines Flavin-Adenine Dinucleotide NADP Molybdenum Iron Oxidoreductases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Nason A
Lee K Y
Pan S S
Ketchum P A
Lamberti A
DeVries J
References (21)
21 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1971-12-00
Pages
3242-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC389631
Subset
IM
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