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Sevilla F, López-Gorgé J, Del Río LA. Characterization of a Manganese Superoxide Dismutase from the Higher Plant Pisum sativum. Plant Physiol. 1982;70(5):1321-6doi: 10.1104/pp.70.5.1321.
Sevilla, F., López-Gorgé, J., & Del Río, L. A. (1982). Characterization of a Manganese Superoxide Dismutase from the Higher Plant Pisum sativum. Plant physiology, 70(5), 1321-6. https://doi.org/10.1104/pp.70.5.1321
Sevilla, F, et al. "Characterization of a Manganese Superoxide Dismutase from the Higher Plant Pisum sativum." Plant physiology vol. 70,5 (1982): 1321-6. doi: https://doi.org/10.1104/pp.70.5.1321
Sevilla F, López-Gorgé J, Del Río LA. Characterization of a Manganese Superoxide Dismutase from the Higher Plant Pisum sativum. Plant Physiol. 1982 Nov;70(5):1321-6. doi: 10.1104/pp.70.5.1321. PMID: 16662674; PMCID: PMC1065882.
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Plant Physiol. 1982 Nov;70(5):1321-6. doi: 10.1104/pp.70.5.1321.

Characterization of a Manganese Superoxide Dismutase from the Higher Plant Pisum sativum.

Plant physiology

F Sevilla, J López-Gorgé, L A Del Río

Affiliations

  1. Unidad de Bioquímica Vegetal, Estación Experimental del Zaidín, C. S. I. C., Profesor Albareda 1, Granada, Spain.

PMID: 16662674 PMCID: PMC1065882 DOI: 10.1104/pp.70.5.1321

Abstract

A manganese-containing superoxide dismutase (EC 1.15.1.1) was fully characterized from leaves of the higher plant Pisum sativum L., var. Lincoln. The amino acid composition determined for the enzyme was compared with that of a wide spectrum of superoxide dismutases and found to have a highest degree of homology with the mitochondrial manganese superoxide dismutases from rat liver and yeast. The enzyme showed an apparent pH optimum of 8.6 and at 25 degrees C had a maximum stability at alkaline pH values. By kinetic competition experiments, the rate constant for the disproportionation of superoxide radicals by pea leaf manganese superoxide dismutase was found to be 1.61 x 10(9) molar(-1).second(-1) at pH 7.8 and 25 degrees C. The enzyme was not sensitive to NaCN or to H(2)O(2), but was inhibited by N(3) (-). The sulfhydryl reagent p-hydroxymercuribenzoate at 1 mm concentration produced a nearly complete inhibition of the manganese superoxide dismutase activity. The metal chelators o-phenanthroline, EDTA, and diethyldithiocarbamate all inhibited activity slightly in decreasing order of intensity. A comparative study between this higher plant manganese superoxide dismutase and other dismutases from different origins is presented.

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