Skip to main content
Plant Physiology logoLink to Plant Physiology
. 1980 May;65(5):984–989. doi: 10.1104/pp.65.5.984

Reduction of Nitrate and Nitrite in Lambsquarters (Chenopodium album) Biotypes Resistant and Susceptible to Atrazine Toxicity 1

John M Lawrence 1, Robert J Foster 1, Hedwig E Herrick 1
PMCID: PMC440462  PMID: 16661320

Abstract

The nitrite-reducing activity of the normal susceptible biotype of lambsquarters (Chenopodium album L.) was strongly inhibited by atrazine in the assay medium, both in the case of the in vivo assays of leaf discs in light, and in vitro photoreduction assays of crude extracts. In vitro assays of crude extracts with methylviologen or ferredoxin supplying the reducing potential were not inhibited by atrazine. In the resistant biotype, inhibition of nitrite reduction did not occur with any of the above assays. Thus, it appears that atrazine does not inhibit nitrite reductase itself, but rather the availability of photosynthetically supplied electrons for the reduction. Atrazine had no effect when added to the media for either in vivo or in vitro assays of nitrate reduction by either the susceptible or resistant biotype.

Young lambsquarters plants were treated with atrazine by spraying the leaves at a rate which was lethal for susceptible plants after 5 or 6 days, but had little effect on the resistant biotype. Nitrite did not accumulate in either biotype, but remained present at the level of about 0.1 microgram nitrite N per gram fresh weight. The nitrate content of susceptible-type leaves did increase to two or three times the initial level, during the first four days after spraying. Usually the only visible effect on the plants during this time was a decreased growth rate. Twenty-four hours after spraying the following activities had fallen to 25% or less of the activities of solvent-sprayed control plants: in vivo nitrite reductase, in vivo nitrate reductase, in vitro NADH-nitrate reductase, in vitro reduced flavin mononucleotidenitrate reductase, and in vitro NADH-diaphorase. In these atrazine-treated plants, in vitro nitrite reductase activity with reducing potential supplied by methylviologen was not affected, nor were any of the above activities in leaves of atrazine-treated resistant plants. The abrupt fall in nitrate reductase represents an effect of atrazine not directly related to inhibition of photosynthesis.

Full text

PDF
984

Selected References

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

  1. Gopinath A., Hill M. S. Deflection beam-chopping in the SEM. J Phys E. 1977 Mar;10(3):229–236. doi: 10.1088/0022-3735/10/3/014. [DOI] [PubMed] [Google Scholar]
  2. Jolly S. O., Tolbert N. E. NADH-Nitrate Reductase Inhibitor from Soybean Leaves. Plant Physiol. 1978 Aug;62(2):197–203. doi: 10.1104/pp.62.2.197. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Joy K. W., Hageman R. H. The purification and properties of nitrite reductase from higher plants, and its dependence on ferredoxin. Biochem J. 1966 Jul;100(1):263–273. doi: 10.1042/bj1000263. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Miflin B. J. The location of nitrite reductase and other enzymes related to amino Acid biosynthesis in the plastids of root and leaves. Plant Physiol. 1974 Oct;54(4):550–555. doi: 10.1104/pp.54.4.550. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Paneque A., Del Campo F. F., Ramírez J. M., Losada M. Flavin nucleotide nitrate reductase from spinach. Biochim Biophys Acta. 1965 Sep 27;109(1):79–85. doi: 10.1016/0926-6585(65)90092-0. [DOI] [PubMed] [Google Scholar]
  6. Schrader L. E., Ritenour G. L., Eilrich G. L., Hageman R. H. Some characteristics of nitrate reductase from higher plants. Plant Physiol. 1968 Jun;43(6):930–940. doi: 10.1104/pp.43.6.930. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Tischler C. R., Purvis A. C., Jordan W. R. Factors Involved in in Vitro Stabilization of Nitrate Reductase from Cotton (Gossypium hirsutum L.) Cotyledons. Plant Physiol. 1978 May;61(5):714–717. doi: 10.1104/pp.61.5.714. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Wallace W. Comparison of a nitrate reductase-inactivating enzyme from the maize root with a protease form yeast which inactivates tryptophan synthase. Biochim Biophys Acta. 1978 Jun 9;524(2):418–427. doi: 10.1016/0005-2744(78)90179-1. [DOI] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES