Advertisement

Redox Components in the Plant Plasma Membrane

  • Ian M. Møller
  • Per Askerlund
  • Christer Larsson
  • Alajos Bérczi
  • Susanne Widell
Part of the NATO ASI Series book series (NSSA, volume 7)

Abstract

As early as 1945, Lundegårdh proposed that redox processes took place in the plasma membrane (PM) of plants. He further envisaged that ion uptake, specifically anion uptake, across the PM of root cells was directly coupled to the flow of electrons to oxygen. This anion respiration was thought to be catalyzed by the respiratory redox components known at that time, mainly the cytochromes. When these around 1950 were discovered to reside in an organelle, the mitochondrion, and not in the PM, the theory of Lundegårdh became less tenable (see Lundegårdh, 1955) and it gradually lost prominence. However, in hindsight we can now see that his main idea was correct — there is at present plenty of evidence that the PM of both animals and plants contains redox components which can participate in a number of redox processes (see Crane et al., 1985a, b; Lüttge and Clarkson, 1985; Møller and Lin, 1986; for comprehensive reviews). In the present review we will critically evaluate the evidence for each redox component proposed to be present in the PM of plants. We will then briefly discuss the possible location of these redox components as well as the various processes they might be involved in.

Keywords

Wheat Root Redox Activity Midpoint Potential Plant Plasma Membrane Salicylhydroxamic Acid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Askerlund, P., Larsson, C., Widell, S., and Miller, I.M., 1987, NAD(P)H oxidase and peroxidase activities in purified plasma membranes from cauliflower inflorescences, Physiol. Plant., 71: 9.CrossRefGoogle Scholar
  2. Askerlund, P., Larsson, C., and Widell, S., 1988, manuscript in preparation.Google Scholar
  3. Barr, R., Sandelius, A.S., Crane, F.L., and Morré, D.J., 1985, Oxidation of reduced nucleotides by plasma membranes of soybean hypocotyl, Biochem. Biophys. Res. Commun., 131: 943.PubMedCrossRefGoogle Scholar
  4. Barr, R., Sandelius, A.S., Crane, F.L., and Morré, D.J., 1986, Redox reactions of tonoplast and plasma membranes isolated from soybean hypocotyls by free-flow electrophoresis, Biochim. Biophys. Acta, 852: 254.PubMedCrossRefGoogle Scholar
  5. Bérczi, A., and Mller, I.M., 1986, Comparison of the properties of plasmalemma vesicles purified from wheat roots by phase partitioning and by discontinuous sucrose gradient centrifugation, Physiol. Plant., 68: 59.CrossRefGoogle Scholar
  6. Bérczi, A., and Møller, I.M., 1987, Mgt+-ATPase activity in wheat root plasmalemma vesicles: Time-dependence and effect of sucrose and detergents, Physiol. Plant., 70: 583.CrossRefGoogle Scholar
  7. Bérczi, A., Larsson, C., Widell, S., and M$ller, I.M., 1988, Separation of wheat root microsomal membranes by counter-current distribution. An evaluation of plasma membrane markers, in “Proc. of the 3rd Int. Symp. ”Structure and Function of Roots“, Nitra, Czechoslovakia (In press).Google Scholar
  8. Bienfait, H.F., 1985, Regulated redox processes at the plasma-lemma of plant root cells and their function in iron uptake, J. Bioenerg. Biomembr., 17: 73.PubMedCrossRefGoogle Scholar
  9. Brain, R.D., Freeberg, J.F., Weiss, C.V., and Briggs, W.R.,1977, Blue light-induced absorbance changes in membrane fractions from corn and Neurospora, Plant Physiol., 57: 948.Google Scholar
  10. Bruder, G., Fink, A., and Jarasch, E.-D., 1978, The b-type cytochrome in endoplasmic reticulum of mammary gland epithelium and milk fat globule membranes consists of two components, cytochrome b5 and cytochrome P-420, Exp. Cell Res., 117: 207.PubMedCrossRefGoogle Scholar
  11. Buckhout, T.J., and Hrubec, T.C., 1986, Pyridine nucleotide-dependent ferricyanide reduction associated with isolated plasma membranes of maize (Zea mays L.) roots, Protoplasma, 135: 144.CrossRefGoogle Scholar
  12. Caubergs, R.J., Asard, H.H., De Greef, J.A., Leeuwerik, F.J., and Oltmann, F.L., 1986, Light-inducible absorbance changes and vanadate-sensitive ATPase activity associated with the presumptive plasma membrane fraction from cauliflower inflorescences, Photochem. Photobiol., 44: 641.CrossRefGoogle Scholar
  13. Craig, T.A., and Crane, F.L., 1981, Evidence for a trans-plasma membrane electron transport system in plant cells, Proc. Indiana Acad. Sci., 90: 150.Google Scholar
  14. Crane, F.L., and Barr, R., 1971, Determination of ubiquinones, Methods Enzymol., 18: 137.CrossRefGoogle Scholar
  15. Crane, F.L., Löw, H., Clark, M.G., 1985a, Plasma membrane redox enzymes, in: The Enzymes of Biological Membranes, A.N. Martonosi, ed., Plenum Press, New York.Google Scholar
  16. Crane, F.L., Sun, I.L., Clark, M.G., Grebing, C., and Löw, H., 1985b, Transplasma-membrane redox systems in growth and development, Biochim. Biophys. Acta, 811: 233.PubMedCrossRefGoogle Scholar
  17. Edman, K., Ericson, I., and Miller, I.M., 1985, The regulation of exogenous NAD(P)H oxidation in spinach leaf mitochondria by pH and cations, Biochem. J., 232: 471.PubMedGoogle Scholar
  18. Ernster, L., Glaser, E., and Norling, B., 1978, Extraction and reincorporation of ubiquinone in submitochondrial particles, Methods Enzymol. 53: 573.PubMedCrossRefGoogle Scholar
  19. Hodges, T.K., and Mills, D., 1986, Isolation of the plasma membrane, Methode Enzymol., 118: 41.CrossRefGoogle Scholar
  20. Jesaitis, A.J., Heners, P.R., Hertel, R., and Briggs, W.R., 1977, Characterization of a membrane fraction containing a b-type cytochrome, Plant Physiol., 59: 941.PubMedCrossRefGoogle Scholar
  21. Kjellbom, P., and Larsson, C., 1984, Preparation and polypeptide composition of chlorophyll-free plasma membranes from leaves of light-grown spinach and barley, Physiol. Plant., 62: 501.CrossRefGoogle Scholar
  22. Kjellbom, P., Larsson, C., Askerlund, P., Schelin, C., and Widell, S., 1985, Cytochrome P-450/420 in plant plasma membranes: A possible component of the blue-light-reducible flavoprotein-cytochrome complex, Photochem. Photobiol., 42: 779.CrossRefGoogle Scholar
  23. Kröger, A., 1978, Determination of contents and redox states of ubiquinone and menaquinone, Methods Enzymol., 53: 579.PubMedCrossRefGoogle Scholar
  24. Larsson, C., 1985, Plasma membranes, in: Cell Components. Modern Methods of Plant Analysis, New Series, Vol. 1, pp. 87–104, H.F. Linskens, J.F. Jackson, eds, Springer-Verlag, Berlin.Google Scholar
  25. Larsson, C., Kjellbom, P., Widell, S., and Lundborg, T., 1984, Sidedness of plant plasma membrane vesicles purified by partition in aqueous polymer two-phase systems, FEBS Lett., 171: 271.CrossRefGoogle Scholar
  26. Larsson, C., Widell, S., and Kjellbom, P., 1987, Preparation of high-purity plasma membranes, Methods Enzymol., 148: 558.CrossRefGoogle Scholar
  27. Larsson, C., Widell, S., and Sommarin, M., 1988, Inside-out plant plasma membrane vesicles of high purity obtained by aqueous two-phase partitioning, FEBS Lett., in press.Google Scholar
  28. Leong, T.-Y., Viestra, R.D., and Briggs, W.R., 1981, A blue light-sensitive cytochrome-flavin complex from corn coleoptiles. Further characterization, Photochem. Photobiol. 34: 697.Google Scholar
  29. Lin, W., 1982, Isolation of NADH oxidation system from the plasmalemma of corn root protoplasts. Plant Physiol., 70: 326.PubMedCrossRefGoogle Scholar
  30. Lin, W., 1984, Further characterization on the transport property of plasmalemma NADH oxidation system in isolated corn root protoplasts, Plant Physiol., 74: 219.PubMedCrossRefGoogle Scholar
  31. LundegArdh, H., 1945, Absorption, transport and exudation of inorganic ions by the roots, Arkiv Bot., 32A (12): 1Google Scholar
  32. Lundegârdh, H., 1955, Mechanisms of absorption, transport, accumulation, and secretion of ions, Annu. Rev. Plant Physiol., 6: 1.CrossRefGoogle Scholar
  33. Lundborg, T., Widell, S., and Larsson, C., 1981, Distribution of ATPases in wheat root membranes separated by phase partition, Physiol. Plant., 52: 89.CrossRefGoogle Scholar
  34. Luster, D.G., and Buckhout, T.J., 1988, Multiple electron transport activities in plasma membranes from maize (Zea mays) roots, Physiol. Plant., in press.Google Scholar
  35. Lüttge, U., and Clarkson, D.T., 1985, Mineral nutrition: Plasmalemma and tonoplast redox activities, Progr. Bot., 47: 73.CrossRefGoogle Scholar
  36. Madyastha, K.M., and Krishnamachary, N., 1986, Purification and partial characterization of microsomal cytochrome b55 from the higher plant Catharanthus roseus, Biochem. Biophys. Res. Commun., 136: 570.PubMedCrossRefGoogle Scholar
  37. Møller, I.M., and Bérczi, A., 1985, Oxygen consumption by purified plasmalemma vesicles from wheat roots. Stimulation by NADH and salicylhydroxamic acid, FEBS Lett., 193: 180.CrossRefGoogle Scholar
  38. Møller, I.M., and Bérczi, A., 1986, Salicylhydroxamic acid-stimulated NADH oxidation by purified plasmalemma vesicles from wheat roots, Physiol. Plant., 68: 67.CrossRefGoogle Scholar
  39. Miller, I.M., and Lin, W., 1986, Membrane-bound NAD(P)H dehydrogenases in higher plant cells, Annu. Rev. Plant Physiol. 37: 309.CrossRefGoogle Scholar
  40. Møller, I.M., Lundborg, T., and Bérczi, A., 1984, The negative surface charge density of plasmalemma vesicles from wheat and oat roots, FEBS Lett., 167: 181.CrossRefGoogle Scholar
  41. Morré, D.J., Crane, F.L., Barr, R., Penel, C., and Wu, L.-Y. 1988, Inhibition of plasma membrane redox activities and elongation growth of soybean, Physiol. Plant., 72: 236.CrossRefGoogle Scholar
  42. Novak, V.A., and Miklashevich, A.I., 1986, Ferricyanide reductase and ferrocyanide oxidase activities of the micro-alga Scenesdesmus acuminatus, Sov. Plant Physiol., 32: 694.Google Scholar
  43. Pupillo, P., Valenti, V., De Luca, L., and Hertel, R., 1986, Kinetic characterization of reduced pyridine nucleotide dehydrogenases (duroquinone-dependent) in Cucurbita microsomes, Plant Physiol., 80: 384.PubMedCrossRefGoogle Scholar
  44. Qui, Z.-S., Rubinstein, B., and Stern, A.I., 1985, Evidence for electron transport across the plasma membrane of Zea mays root cells, Planta, 165: 383.CrossRefGoogle Scholar
  45. Ramirez, J.M., Gallego, G.G., and Serrano, R., 1984, Electron transfer constituents in plasma membrane fractions of Avena sativa and Saccharomyces cerevisiae, Plant Sci. Lett., 34:103.Google Scholar
  46. Rubinstein, B., and Stern A.I., 1986, Relationship of transplasmalemma redox activity to proton and solute transport by roots of Zea mays., Plant Physiol., 80: 805.PubMedCrossRefGoogle Scholar
  47. Sandelius, A.S., Penel, C., Auderset, G., Brightman, A.,Millard, M., and Morré, D.J., 1986a, Isolation of highly purified fractions of plasma membrane and tonoplast from the same homogenate of soybean hypocotyls by free-flow electrophoresis, Plant Physiol., 81: 177.Google Scholar
  48. Sandelius, A.S., Barr, R., Crane, F.L., and Morré, D.J., 1986b, Redox reactions of plasma membranes isolated from soybean hypocotyls by phase partition, Plant Sci., 48: 1CrossRefGoogle Scholar
  49. Sijmons, P.C., van den Briel, W., and Bienfait, H.F., 1984a, Cytosolic NADPH is the electron donor for extracellular FeIII reduction in iron-deficient bean roots, Plant Physiol., 75: 219.PubMedCrossRefGoogle Scholar
  50. Sijmons, P.C., Lanfermeijer, F.C., de Boer, A.H., Prins, H.B.A., and Bienfait, H.F., 1984b, Depolarization of cell membrane potential during trans-plasma membrane electron transfer to extracellular electron acceptors in iron-deficient roots of Phaseolus vulgaris L., Plant Physiol., 76: 943.PubMedCrossRefGoogle Scholar
  51. Widell, S., 1987, Membrane-bound blue light receptors -Possible connection to blue light photomorphogenesis, pp. 89–98, in: Blue Light Responses: Phenomena and Occurrence in Plants and Microorganisms, Vol. II, H. Senger, ed., CRC Press, Boca Raton, FL.Google Scholar
  52. Widell, S., and Larsson, C., 1981, Separation of presumptive plasma membranes from mitochondria by partition in an aqueous polymer two-phase system, Physiol. Plant., 51: 368.CrossRefGoogle Scholar
  53. Widell, S., and Larsson, C., 1983, Distribution of cytochrome b photoreductions mediated by endogenous photosensitizers or methylene blue in fractions from corn and cauliflower, Physiol. Plant., 57: 196.CrossRefGoogle Scholar
  54. Widell S., Caubergs, R.J. and Larsson, C., 1983, Spectral characterization of light-reducible cytochrome in a plasma membrane-enriched fraction and in other membranes from cauliflower inflorescences, Photochem. Photobiol., 38: 95.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Ian M. Møller
    • 1
  • Per Askerlund
    • 1
  • Christer Larsson
    • 1
  • Alajos Bérczi
    • 2
  • Susanne Widell
    • 1
  1. 1.Department of Plant PhysiologyUniversity of LundLundSweden
  2. 2.Institute of Biophysics, Biological Research CenterHungarian Academy of ScienceSzegedHungary

Personalised recommendations