, Volume 217, Issue 1–3, pp 70–76 | Cite as

Interaction between electron transport at the plasma membrane and nitrate uptake by maize (Zea mays L.) roots

  • D. Steffen
  • O. Döring
  • M. A. Busch
  • M. Böttger
  • S. Lüthje


In the present study nitrate uptake by maize (Zea mays L.) roots was investigated in the presence or absence of ferricyanide (hexacyanoferrate III) or dicumarol. Nitrate uptake caused an alkalization of the medium. Nitrate uptake of intact maize seedlings was inhibited by ferricyanide while the effect of dicumarol was not very pronounced. Nitrite was not detected in the incubation medium, neither with dicumarol-treated nor with control plants after application of 100 μM nitrate to the incubation solution. In a second set of experiments interactions between nitrate and ferricyanide were investigated in vivo and in vitro. Nitrate (1 or 3 mM) did neither influence ferricyanide reductase activity of intact maize roots nor NADH-ferricyanide oxidoreductase activity of isolated plasma membranes. Nitrate reductase activity of plasma-membrane-enriched fractions was slightly stimulated by 25 μM dicumarol but was not altered by 100 μM dicumarol, while NADH-ferricyanide oxidoreductase activity was inhibited in the presence of dicumarol. These data suggest that plasma-membrane-bound standard-ferricyanide reductase and nitrate reductase activities of maize roots may be different. A possible regulation of nitrate uptake by plasmalemma redox activity, as proposed by other groups, is discussed.


Plasma membrane Redox activity Nitrate reductase Nitrate uptake Zea mays Ferricyanide reductase 



alcohol dehydrogenase


hexacyanoferrate III (ferricyanide)


NADP-dependent malic enzyme


nitrate reductase


plasma membrane


nitrate reductase copurifying with plasma membranes


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  1. Askerlund P, Laurent P, Nakagawa H, Kader JC (1991) NADH-ferricyanide reductase of leaf plasma membranes: partial purification and immunological relation to potato tuber microsomal NADH-ferricyanide reductase and spinach leaf NADH-nitrate reductase. Plant Physiol 96: 1178–1184Google Scholar
  2. Barr R, Böttger M, Crane FL, Morré DJ (1995) Nitrate reductase activity of plasma membranes from cultured carrot cells. Protoplasma 184: 151–157Google Scholar
  3. Bienfait HF (1985) Regulated redox processes at the plasmalemma of plant root cells and their function in iron uptake. J Bioenerg Biomembr 17: 73–83Google Scholar
  4. Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72: 248–254Google Scholar
  5. Busch MA, Böttger M (1997) Net proton secretion as a parameter for nitrate uptake. Protoplasma 196: 65–68Google Scholar
  6. Chen J, Wang JH (1994) Ferricyanide reductase in plasma membranes of maize roots. Acta Phytophysiol Sin 20: 69–76Google Scholar
  7. — — (1995) Existence and characteristics of nitrate reductase in plasma membrane of maize roots. Sci China Ser B Chem Life Sci Earth 38: 564–572Google Scholar
  8. Corzo A, Plasa R, Ullrich WR (1991) Extracellular ferricyanide reduction and nitrate reductase activity in the green algaMonoraphidium braunii. Plant Sci 75: 221–228Google Scholar
  9. Crawford NM (1995) Nitrate: nutrient and signal for plant growth. Plant Cell 7: 859–868Google Scholar
  10. Danner J, Ting IP (1967) CO2 metabolism in corn roots II: intracellular distribution of enzymes. Plant Physiol 42: 719–724Google Scholar
  11. Döring O, Lüthje S (1996) Molecular components and biochemistry of plant plasma membrane oxidoreductases. Mol Membr Biol 13: 127–142Google Scholar
  12. — —, Hilgendorf F, Böttger M (1990) Membrane depolarization by hexacyanoferrate (III), hexabromoiridate (IV) and hexachloroiridate (IV). J Exp Bot 41: 1055–1061Google Scholar
  13. — —, Böttger M (1992) Modification of the activity of the plasma membrane redox system ofZea mays L. roots by vitamin K3 and dicumarol. J Exp Bot 43: 175–181Google Scholar
  14. —, Busch M, Lüthje S, Lüthen H, Hilgendorf F, Böttger M (1996) Ionostats. Protoplasma 194: 1–10Google Scholar
  15. —, Böttger M, Lüthje S (1998) To be or not to be: a question of plasma membrane redox. Prog Bot 59: 328–354Google Scholar
  16. Gallagher SR, Leonard RT (1982) Effect of vanadate and azide on membrane-associated ATPase and soluble phosphatase activites of corn roots. Plant Physiol 70: 1335–1340Google Scholar
  17. Glass ADM (1988) Nitrogen uptake by plant roots. ISI Atlas Sci Animal Plant Sci 1: 151–156Google Scholar
  18. Hoarau J, Nato A, Lavergne D, Flipo V, Hirel B (1991) Nitrate reductase activity changes during a culture cycle of tobacco cells: the participation of a membrane-bound form enzyme. Plant Sci 79: 193–204Google Scholar
  19. Hu P, Murphy TM (1996) Ferricyanide reductase of rose plasma membranes is regulated by nitrogen supply. Plant Cell Rep 15: 833–835Google Scholar
  20. Jones GJ, Morel FMM (1988) Plasmalemma redox activity in the diatomThalassiosira. Plant Physiol 87: 143–147Google Scholar
  21. Kuschel L, Dahse I, Müller E (1996) Lack of correlation between transplasmalemma electron transport rate and depolarization inEgeria densa leaf cells. J Plant Physiol 147: 675–684Google Scholar
  22. Lüthje S, Böttger M (1995) On the function of a K-type vitamin in plasma membranes of maize (Zea mays L.) roots. Mitt Inst Allg Bot Hamburg 25: 5–13Google Scholar
  23. —, Döring O, Böttger M (1992) The effects of vitamin K3 and dicumarol on the plasma membrane redox system and H+ pumping activity ofZea mays L. roots measured over a long time scale. J Exp Bot 43: 183–188Google Scholar
  24. —, Gonzalés-Reyes JA, Navas P, Döring O, Böttger M (1994) Inhibition of maize (Zea mays L.) root plasma membrane-bound redox activities by coumarins. Z Naturforsch 49c: 447–452Google Scholar
  25. —, Döring O, Heuer S, Lüthen H, Böttger M (1997) Plant plasma membrane oxidoreductases. Biochim Biophys Acta 1331: 81–102Google Scholar
  26. L'Vov NP, Safaraliev PM (1988) Methods of determining nitrate activtiy in plants. Sov Plant Physiol 35: 154–157Google Scholar
  27. Marco A, Jia C, Fischer-Schliebs E, Varanini Z, Lüttge U (1994) Evidence for two different nitrate-reducing activities at the plasma membrane in roots ofZea mays L. Planta 194: 557–564Google Scholar
  28. Racker E (1955) Alcohol dehydrogenase from baker's yeast. In: Colowick SP, Kaplan NO (eds) Methods of enzymology, vol 1. Academic Press, New York, pp 500–503Google Scholar
  29. Scagliarini S, Pupillo P, Valenti V (1988) Isoforms of NADP-dependent malic enzyme in tissues of the greening maize leaf. J Exp Bot 39: 1109–1119Google Scholar
  30. Scholl RL, Harper JE, Hageman RH (1974) Improvements of the nitrite color development in assays of nitrate reductase by phenazine methosulfate and zinc acetate. Plant Physiol 53: 825–828Google Scholar
  31. Smarelli J, Campbell WH (1979) NADH dehydrogenase activity of higher plant nitrate reductase (NADH). Plant Sci Lett 16: 139–147Google Scholar
  32. Stöhr C, Glogau U, Matschke M, Tischner R (1995) Evidence for the involvement of plasma-membrane-bound nitrate reductase in signal transduction during blue-light stimulation of nitrate uptake inChlorella saccharophila. Planta 197: 613–618Google Scholar
  33. Tischner R, Waldeck B, Goyal SS, Rains WS (1993) Effect of nitrate pulses on the nitrate-uptake rate, synthesis of mRNA coding for nitrate reductase, and nitrate-reductase activity in the roots of barley seedlings. Planta 189: 533–537Google Scholar
  34. Ullrich WR, Novacky A (1981) Nitrate-dependent membrane potential changes and their induction inLemna gibba G1. Plant Sci Lett 22: 211–217.Google Scholar
  35. Ward MR, Tischner R, Huffaker RC (1988) Inhibition of nitrate transport by anti-nitrate reductase IgG fragments and the identification of plasma membrane associated nitrate reductase in roots of barley seedlings. Plant Physiol 88: 1141–1145Google Scholar
  36. Witt FG, Aparicio PJ (1995) Characterization of the blue light-induced extracellular alkalization associated with monovalent anion uptake byMonoraphidium braunii: competition between NO3 and Cl. Physiol Plant 94: 545–552Google Scholar

Copyright information

© Springer-Verlag 2001

Authors and Affiliations

  • D. Steffen
    • 1
  • O. Döring
    • 1
  • M. A. Busch
    • 1
  • M. Böttger
    • 1
  • S. Lüthje
    • 1
  1. 1.Institut für Allgemeine BotanikUniversität HamburgHamburgFederal Republic of Germany

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