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A plasma membrane-bound enzyme of tobacco roots catalyses the formation of nitric oxide from nitrite
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A plasma membrane-bound enzyme of tobacco roots catalyses the formation of nitric oxide from nitrite
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Journal Article
A plasma membrane-bound enzyme of tobacco roots catalyses the formation of nitric oxide from nitrite
2001
Overview
Purified plasma membranes (PMs) of tobacco (Nicotiana tabacum L. cv. Samsun) roots exhibited a nitrite-reducing enzyme activity that resulted in nitric oxide (NO) formation. This enzyme activity was not detected in soluble protein fractions or in PM vesicles of leaves. At the pH optimum of pH 6.0, nitrite was reduced to NO with reduced cytochrome c as electron donor at a rate comparable to the nitrate-reducing activity of root-specific succinate-dependent PM-bound nitrate reductase (PM-NR). The hitherto unknown PM-bound nitrite: NO-reductase (NI-NOR) was insensitive to cyanide and anti-NR IgG and thereby proven to be different from PM-NR. Furthermore, PM-NR and NI-NOR were separated by gel-filtration chromatography and apparent molecular masses of 310 kDa for NI-NOR and 200 kDa for PM-NR were estimated. The PM-associated NI-NOR may reduce the apoplastic nitrite produced by PM-NR in vivo and may play a role in nitrate signalling via NO formation.
Publisher
Springer-Verlag,Springer
Subject
Agronomy. Soil science and plant productions
/ Biological and medical sciences
/ Electron Transport Complex IV - metabolism
/ Enzymes
/ Fundamental and applied biological sciences. Psychology
/ Immunoglobulin G - pharmacology
/ Nitrate Reductases - metabolism
/ Nitrates
/ Nitrite Reductases - metabolism
/ Nitrites
/ Nitrogen
/ Nitrogen metabolism and other ones (excepting carbon metabolism)
/ Nutrition. Photosynthesis. Respiration. Metabolism
/ Oxides
/ Oxidoreductases - isolation & purification
/ Oxidoreductases - metabolism
/ Plant physiology and development
/ Plants
/ roots
