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. 1986 Jan;80(1):72–76. doi: 10.1104/pp.80.1.72

Nitrate Reductases from Wild-Type and nr1-Mutant Soybean (Glycine max [L.] Merr.) Leaves 1

II. Partial Activity, Inhibitor, and Complementation Analyses

Richard S Nelson 1,2,2, Luc Streit 1,2, James E Harper 1,2
PMCID: PMC1075059  PMID: 16664611

Abstract

Soybean (Glycine max [L.] Merr.) leaves have been shown to contain three forms of nitrate reductase (NR). Two of the forms, which are present in leaves of wild-type (cv. Williams) plants grown in the absence of NO3−, are termed constitutive and designated c1NR and c2NR. The third form, which is present in NO3−-grown mutant (nr1) plants lacking the constitutive forms, is termed inducible and designated iNR. Samples of c1NR, c2NR, and iNR obtained from appropriately treated plants were analyzed for the presence of partial activities, response to inhibitors, and ability to complement a barley NR which lacks the molybdenum cofactor (MoCo) but is otherwise active.

The three forms were similar to most assimilatory NR enzymes in that they (a) exhibited NADH-cytochrome c reductase, reduced flavin mononucleotide-NR, and reduced methyl viologen-NR partial activities; (b) were inhibited by p-hydroxymercuribenzoate at the site of initial electron transport through each enzyme; (c) were more inhibited by CN− in their reduced enzyme state as compared with their oxidized state; and (d) complemented a MoCo-defective NR (e.g. contained cofactors with characteristics similar to the MoCo found in barley NR and commercial xanthine oxidase). However, among themselves, they showed dissimilarities in their response to treatment with HCO3− and CN−, and in their absolute ability to complement the barley NR. The site of effect for these treatments was the terminal cofactor-containing portion of each enzyme. This indicated that, although a terminal cofactor (presumably a MoCo) was present in each form, structural or conformational differences existed in the terminal cofactor-protein complex of each form.

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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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