A plasma membrane-bound enzyme of tobacco roots catalyses the formation of nitric oxide from nitrite

Planta. 2001 Apr;212(5-6):835-41. doi: 10.1007/s004250000447.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalysis
  • Cell Membrane / metabolism
  • Electron Transport
  • Electron Transport Complex IV / metabolism*
  • Hydrogen-Ion Concentration
  • Immunoglobulin G / pharmacology
  • Nitrate Reductases / metabolism
  • Nitrates / metabolism
  • Nitric Oxide / metabolism*
  • Nitrite Reductases / metabolism
  • Nitrites / metabolism*
  • Oxidation-Reduction
  • Oxidoreductases / isolation & purification
  • Oxidoreductases / metabolism*
  • Plant Roots / drug effects
  • Plant Roots / enzymology
  • Plants, Toxic*
  • Signal Transduction
  • Succinic Acid / metabolism
  • Tobacco / enzymology*


  • Immunoglobulin G
  • Nitrates
  • Nitrites
  • Nitric Oxide
  • Succinic Acid
  • Oxidoreductases
  • Nitrate Reductases
  • Nitrite Reductases
  • nitric-oxide reductase
  • Electron Transport Complex IV