Molecular components and biochemistry of electron transport in plant plasma membranes (Review)

REFERENCES

• Ahmad M., Cashmore A. R. HY4 gene of A. thaliana encodes a protein with characteristics of a blue light photoreceptor. Nature 1993; 366: 162–166
   PubMed Web of Science ®Google Scholar
• Allen J. F., Alexciev K., Hakansson G. Regulation by redox signaling. Current Biology 1995; 3: 869–872
   Google Scholar
• Anderson A. J., Rogers K., Tepper C. S., Blee K., Cardon J. Timing of molecular events following elicitor treatment of plant cells. Physiological and Molecular Plant Pathology 1991; 38: 1–13
   Google Scholar
• Anraku Y. Bacterial electron transport chains. Annual Reviews in Biochemistry 1988; 57: 101–132
   PubMedGoogle Scholar
• Arrigoni O. Ascorbate system in plant development. Journal of Bioenergetics and Biomembranes 1994; 26: 407–419
   PubMed Web of Science ®Google Scholar
• Arrigoni O., Dipierro S., Borraccino G. Ascorbate freeradical redical reductase, a key enzyme of the ascorbic acid system. FEBS Letters 1981; 125: 242–245
   Google Scholar
• Asard H., Caubergs R. LIAC activity in higher plants. In Biophysics of Photoreceptors and Photomovement in Microorganisms, F. Lenci, F. Ghetti, G. Colombetti, D. P. Häder, P. S. Song. NATO ASI Series 211, 1990; 181–189
   Google Scholar
• Asard H., Caubergs R., Renders D., DeGreef J. A. Duroquinone stimulated NADH oxidase and b-type cytochromes in the plasma membrane of cauliflower and mung beans. Plant Science 1987; 53: 109–119
   Google Scholar
• Asard H., Venken M., Caubergs R., Reijnders W., Oltmann F. L., DeGreef J. A. b-type cytochromes in higher plant plasma membranes. Plant Physiology 1989; 90: 1077–1083
   PubMed Web of Science ®Google Scholar
• Asard H., Horemans N., Caubergs R. J. Transmembrane electron transport in ascorbate-Ioaded plasma membrane vesicles from higher plants involved a b-type cytochrome. FEBS Letters 1992; 306: 143–146
   Google Scholar
• Asard H., Horemans N., Mertens J., Caubergs R. J. The plant plasma membrane b-type cytochrome: an overview. Belgian Journal of Botany 1994; 127: 171–183
   Google Scholar
• Asard H., Horemans N., Briggs W. R., Caubergs R. J. Blue light perception by endogenous redox components of the plant plasma membrane. Photochemistry and Photobiology 1995; 61: 518–522
   Google Scholar
• Asard H., Horemans N., Caubergs R. J. Involvement of ascorbic acid and a b-type cytochrome in plant plasma membrane redox reactions. Protoplasma 1995; 184: 36–41
   Google Scholar
• Askerlund P., Larsson C. Transmembrane electron transport in plasma membrane vesicles loaded with an NADH-generating system or ascorbate. Plant Physiology 1991; 96: 1178–1184
   PubMedGoogle Scholar
• Askerlund P., Larsson C., Widell S., Møller I. M. NAD(P)H oxidase and peroxidase activities in purified plasma membranes from cauliflower inflorescences. Physiologia Plantarum 1987; 71: 9–19
   Web of Science ®Google Scholar
• Askerlund P., Larsson C., Widell S. Localization of donor and acceptor sites of NADH dehydrogenase activities using insideout and right-side-out plasma membrane vesicles from plants. FEBS Letters 1988; 239: 23–28
   Web of Science ®Google Scholar
• Askerlund P., Larsson C., Widell S. Cytochromes of plant plasma membranes. Characterization by absorbance difference spectrometry and redox titration. Physiologia Plantarum 1989; 76: 123–134
   Web of Science ®Google Scholar
• Askerlund P., Laurent P., Nakagawa H., Kader J. C. NADH-ferricyanide reductase of leaf plasma membranes. Plant Physiology 1991; 95: 6–13
   Google Scholar
• Avery'anoff A. A. Superoxide radical generation by intact pea plants. Soviet Plant Physiology 1985; 32: 202–206
   Google Scholar
• Awad F., Römheld V., Marschner H. Effect of root exudates on mobilization in the rhizosphere and uptake of iron by wheat plants. Plant and Soil 1994; 165: 213–218
   Web of Science ®Google Scholar
• Bagnaresi P., Pupillo P. Characterization of NADH-dependent Fe3 -chelate reductase of maize roots. Journal of Experimental Botany 1995; 46: 1497–1503
   Web of Science ®Google Scholar
• Bagnaresi P., Basso B., Pupillo P. Characterization of NADH ferric-chelate reductases of maize roots. International Conference of Bioiron (ICBI). Asheville, North Carolina 16–21 April, 1995; 79
   Google Scholar
• Barr R. The effect of inhibitors of plasma membrane redox reactions on proton excretion by plant cells. Physiologia Plantarum 1988; 73: 194–199
   Web of Science ®Google Scholar
• Barr R., Sandelius A. S., Crane F. L., Morré D. J. Redox reactions of tonoplast and plasma membranes isolated from soybean hypocotyls by free-flow electrophoresis. Biochimica et Biophysica Acta 1986; 852: 254–261
   PubMed Web of Science ®Google Scholar
• Barr R., Brightman A., Morré D. J., Crane F. L. Modulation of plasma membrane electron transport reactions and associated proton excretion by vitamin K1 and related naphthoquinones. Journal of Cell Biology 1990; 111: 72a, (abstract No. 389)
   Google Scholar
• Barr R., Pan R. S., Crane F. L., Brightman A. O., Morré D. J. Destruction of vitamin K1 of cultured carrot cells by ultraviolet radiation and its effect on plasma membrane electron transport reactions. Biochemistry International 1992; 27: 449–456
   PubMedGoogle Scholar
• Barr R., Böttger M., Crane F. L. The effect of boron on plasma membrane electron transport and associated proton secretion by cultured carrot cells. Biochemistry and Molecular Biology International 1993; 31: 31–39
   Google Scholar
• Barr R., Böttger M., Crane F. L., Morré D. J. Nitrate reductase activity of plasma membranes from cultured carrot cells. Protoplasma 1995; 184: 151–157
   Google Scholar
• Barret M., Maxson J. M. Naphthalic anhydride induces imazethapyr metabolism and cytochrome P-450 activity in maize. Zeitschrift für Naturforschung 1991; 46c: 879–900
   Google Scholar
• Basso B., Bagnaresi P., Bracale M., Soave C. The yellow-stripe-1 and -3 mutants of maize: nutritional and biochemical studies. Maydica 1994; 39: 97–105
   Google Scholar
• Basu P. S., Tuli V. The binding of indol-3-acetic acid and 3-methyleneoxindole to plant macromolecules. Plant Physiology. 1972; 50: 507–509
   Google Scholar
• Belkoura M., Ranjeva R., Marigio G. Cations stimulate proton pumping in Catharanthus roseus cells: implication of a redox system?. Plant, Cell Environment. 1986; 9: 653–656
   Google Scholar
• Benov L. C., Antonov P. A., Ribarov S. R. Oxidative damage of the membrane lipids after electroporation. General Physiology and Biophysics 1994; 13: 85–87
   PubMed Web of Science ®Google Scholar
• Bérczi A., Asard H. NAD(P)H-utilizing oxidoreductases of the plasma membrane. An overview of presently purified proteins. Protoplasma 1995; 184: 140–144
   Google Scholar
• Bérczi A., Brightman A. O. NADH-ferricyanide oxidoreductase is present on both sides of the plant plasma membrane. Plant Science 1994; 97: 47–52
   Google Scholar
• Bérczi A., Fredlund K. M., Møller I. M. Purification and characterization of an NADH-hexacyanoferrate(Ill) reductase from spinach leaf plasma membrane. Archives of Biochemistry and Biophysics 1995; 320: 65–72
   Google Scholar
• Berger F., Brownlee C. Photopolarization of the Fucus sp. zygote by blue light involves a plasma membrane redox chain. Plant Physiology 1994; 105: 519–527
   PubMed Web of Science ®Google Scholar
• Bernstein M., Dahse I. Redox reactions at the plasma membrane of plants. Vom Organismus zum Molekul. Festschrift für Eberhard Müller zum 60. Geburtstag, I. Dahse. Friedrich Schiller Universität Jena. 1992; 52–119
   Google Scholar
• Bernstein M., Dahse I., Müller E., Petzold U. The membrane potential as indicator for transport and energetic processes of leaf cells of the aquatic plant Egeria densa. Biochemie und Physiologie der Pflanzen 1989; 185: 343–356
   Google Scholar
• Bienfait H. F., Lüttge U. On the function of two systems that can transfer electrons across the plasma membrane. Plant Physiology and Biochemistry 1988; 26: 665–671
   Web of Science ®Google Scholar
• Bienfait H. F. Regulated redox processes at the plasmalemma of plant root cells and their function in iron uptake. Journal of Bioenergetics and Biomembranes 1985; 17: 73–83
   PubMed Web of Science ®Google Scholar
• Bolwell G. P., Butt V. S., Davies D. R., Zimmerlin A. The origin of the oxidative burst in plants. Free Radical Research. 1995; 23: 517–532
   PubMed Web of Science ®Google Scholar
• Böttger M., Hilgendorf F. Hormone action on transmembrane electron and H' -transport. Plant Physiology 1988; 86: 1038–1043
   PubMed Web of Science ®Google Scholar
• Böttger M., Lüthen H. Possible linkage between NADH oxidation and proton secretion in Zea mays L. roots. Journal of Experimental Botany 1986; 37: 666–675
   Web of Science ®Google Scholar
• Böttger M., Bigdon M., Soll H. Net proton transport in sunflower hypocotyls: comparative studies of inhibitors. Zeitschrift für Pflanzenphysiologie 1984; 114: 467–475
   Google Scholar
• Böttger M., Barr R., Döring O., Crane F. L., Brightman A. O., Morré D. J. The effects of calcium and calmodulin inhibitors on NADH oxidation by isolated plasma membrane vesicles preloaded with NADH. Plant Science 1992; 87: 39–44
   Google Scholar
• Böttger M., Morré D. J., Crane F. L. Evidence for transmembrane electron transfer coupled to proton secretion in plasma membrane vesicles loaded by electroporation. Protoplasma 1995; 184: 22–30
   Google Scholar
• Bown A. W., Crawford L. A. Evidence that H efflux stimulated by redox activity is independent of plasma membrane ATPase activity. Physiologia Plantarum 1988; 73: 170–174
   Web of Science ®Google Scholar
• Boyer P. D., Krebs E. G. Control by phosphorylation. The Enzymes. Academic Press, Orlando, FL 1986; 3: 322–329, XVII
   Google Scholar
• Brightman A. O., Barr R., Crane F. L., Morré D. J. Auxinstimulated NADH oxidase purified from plasma membrane of soybean. Plant Physiology 1988; 86: 1264–1269
   PubMed Web of Science ®Google Scholar
• Brivet-Chevillote P., di Rago J. P. Electron-transfer by vitamin K3 in a complex Ill-deficient mutant of S. cerevisiae and sequence of the corresponding cytochrome b mutation. FEBS Letters 1989; 255: 5–9
   Google Scholar
• Brown J. C., Ambler J. E. Iron-stress response in tomato (Lycopersicon esculentum). 1. Sites of Fe reduction, absorption and transport. Physiologia Plantarum 1974; 31: 221–224
   Web of Science ®Google Scholar
• Buckhout T. J., Luster D. G. Pyridine nucleotide-dependent reductases of the plant plasma membrane. Oxidoreduction at the Plasma Membrane: Relation to Growth and Transport, F. L. Crane, D. J. Morré, H. E. Löw. CRC Press, Boston, MA 1991; 2: 61–84
   Google Scholar
• Buckhout T. J., Bell P. F., Luster D. G., Chaney R. L. Iron-stress induced redox activity in tomato (Lycopersicum esculentum Mill.) is localized on the plasma membrane. Plant Physiology 1989; 90: 151–156
   PubMed Web of Science ®Google Scholar
• Cakmak I., Marschner H. Zinc-dependent changes in ESR signals, NADPH oxidase and plasma membrane permeability in cotton roots. Physiologia Plantarum 1988; 73: 182–186
   Web of Science ®Google Scholar
• Carrasco-Luna J., Calatayud F., Gonzáles-Darós F., delValle-Tascon S. Hexacyanoferrate (III) stimulation of elongation in coleoptile segments from Zea mays L. Protoplasma 1995; 184: 63–71
   Web of Science ®Google Scholar
• Caubergs R. J., Widell S., Larsson C., DeGreef J. A. Comparison of two methods for the preparation of a membrane fraction of cauliflower inflorescences containing a blue light reducible b-type cytochrome. Physiologia Plantarum 1983; 57: 291–295
   Google Scholar
• Caubergs R. J., Asard H., DeGreef J. A., Leeuwerik F. J., Oltmann F. L. Light-inducible absorbance changes and vanadate-sensitive ATPase activity associated with the presumptive plasma membrane fraction from cauliflower inflorescences. Photochemistry and Photobiology 1986; 44: 641–649
   Web of Science ®Google Scholar
• Cavelier G. Are electron-transport and electron-transfer involved in intracellular signaling?. Medical Hypothesis 1995; 44: 261–262
   Google Scholar
• Chen J., Wang X. C. Existence and characteristics of nitrate reductase in plasma membrane of maize roots. Science in China, Series B—Chemistry Life Sciences and Earth Sciences 1995; 38: 564–572
   Google Scholar
• Cooper J. B., Varner J. E. Cross-linking of soluble extensin in isolated cell walls. Plant Physiology 1984; 76: 414–417
   PubMed Web of Science ®Google Scholar
• Córdoba F., Gonzáles-Reyes J. A. Ascorbate and plant cell growth. Journal of Bioenergetics and Biomembranes 1994; 26: 399–405
   Google Scholar
• Corzo A., Plasa R., Ullrich W. R. Extracellular ferricyanide reduction and nitrate reductase activity in the green alga Monoraphidium braunii. Plant Science 1991; 75: 221–228
   Google Scholar
• Craig T. A., Crane F. L. Evidence for a transplasma membrane electron transport system in plant cells. Proceedings of the Indiana Academy of Science 1981; 90: 150–155
   Google Scholar
• Craig T. A., Crane F. L. Redox potential of the redox donor and the H? release of transplasmalemma redox system of carrot cells. Plant Physiology Supplement 1985; 77: 4
   Google Scholar
• Cramer W. A., Furbacher N., Szczepaniak A., Tae G. S. Electron transport between photosystem II and photosystem I. Current Topics in Bioenergetics 1991; 16: 179–222
   Google Scholar
• Crane F. L., Barr R., Craig T. A., Misra P. C. Growth control by proton pumping plasma membrane redox. Proceedings of the Plant Growth Regulation Society of America 1984; 11: 87–95
   Google Scholar
• Crane F. L., Morré D. J., Löw H. E., Böttger M. The oxidoreductase enzyme in plant plasma membrane. Oxidoreduction at the Plasma Membrane: Relation to Growth and Transport, F. L. Crane, D. J. Morré, H. E. Löw. CRC Press, Boston, MA 1991; 2: 21–33
   Google Scholar
• Crane F. L., Barr R., Brightman A. O., Morré D. J. Vitamin K. A potential switching point in transplasma membrane ferric reductase. Plant Iron Meeting. Logan, Utah 1991; 34
   Google Scholar
• Crane F. L., Sun I. L., Sun E. E., Crowe R. A. Plasma membrane redox and regulation of cell growth. Protoplasma 1995; 184: 3–7
   Web of Science ®Google Scholar
• Crawford N. M. Nitrate: nutrient and signal for plant growth. Plant Cell 1995; 7: 859–868
   PubMed Web of Science ®Google Scholar
• Dancis A., Roman D. G., Anderson G. J., Hinnebusch A. G., Klaussner R. D. Ferric reductase of Saccharomyces cerevisiae: molecular characterization, role in iron uptake, and transcription control by iron. Proceedings of the National Academy of Sciences, USA 1992; 89: 3869–3873
   PubMed Web of Science ®Google Scholar
• Doke N., Miura Y., Chai H. B., Kawakita K. Involvement of active oxygen in induction of plant defense response against infection and injury. Current Topics in Plant Physiology: An American Society of Plant Physiology Series 1991; 6: 84–96
   Google Scholar
• Döring O., Lüthje S., Hilgendorf F., Böttger M. Membrane depolarization by hexacyanoferrate (III), hexabromoiridate (IV) and hexachloroiridate (IV). Journal of Experimental Botany 1990; 43: 1055–1061
   Google Scholar
• Döring O., Lüthje S. Inhibition of trans-plasma membrane oxidoreductase activity and proton secretion of maize (Zea mays L.) roots by coumarins and thenoyltrifluoroacetone in vivo. International Symposium on Plant Membrane Biology. Sparta Center, Lund, Sweden 26–29 April, 1994, 1994(abstract No. P31)
   Google Scholar
• Döring O., Lüthje S., Böttger M. Modification of the activity of the plasma membrane redox system of Zea mays L. roots by vitamin K3 and dicumarol. Journal of Experimental Botany 1992; 43: 175–181
   Google Scholar
• Döring O., Lüthje S., Böttger M. Inhibitors of the plasma membrane redox system of Zea mays L. roots. The vitamin K antagonists dicumarol and warfarin. Biochimica et Biophysica Acta 1992; 1110: 235–238
   Google Scholar
• Federicio R., Giartosio C. E. A trans-plasma membrane electron transport system in maize roots. Plant Physiology 1983; 29: 511–566
   Google Scholar
• Ferrol N., Donaire J. P. Effect of boron on plasma membrane proton extrusion and redox activity in sunflower cells. Plant Science 1992; 86: 41–47
   Web of Science ®Google Scholar
• Fredlund K. M., Struglics A., Widell S., Askerlund P., Kader J. C., Møller I. M. Comparison of the stereospecificity and immunoreactivity of NADH-ferricyanide reductases in plant membranes. Plant Physiology 1994; 106: 1103–1106
   Google Scholar
• Galland P., Senger H. Flavins as possible blue light photoreceptors. Photoreceptor Evolution and Function, M. G. Holmes. Academic Press, London 1991; 65–124
   Google Scholar
• Giannini J. L., Briskin D. P. Pyridine nucleotide oxidation by a plasma membrane fraction from red beet (Beta vulgaris L.) storage tissue. Archives of Biochemistry and Biophysics 1988; 260: 653–660
   Google Scholar
• Goldbach H. E., Hartmann D., Rotzer T. Boron is required for stimulation of ferricyanide-induced H1 -release in suspension cultured cells of Daucus carota and Lycopersicon esculentum. Physiologia Plantarum 1990; 80: 114–118
   Google Scholar
• Goldenberg H. Plasma membrane redox activities. Biochimica et Biophysica Acta 1982; 694: 203–223
   Google Scholar
• Gonzáles-Reyes J. A., Döring O., Navas P., Obst G., Böttger M. The effect of ascorbate free radical on the energy state of the plasma membrane of onion (Allium cepa L.) root cells: alteration of K' efflux by ascorbate?. Biochemica et Biophysica Acta 1992; 1098: 177–183
   Google Scholar
• González-Reyes J. A., Alcain F. J., Caler J. A., Serrano A., Córdoba F., Navas P. Stimulation of root elongation by ascorbate and ascorbate free radical in Allium cepa L. Protoplasma 1995; 184: 31–35
   Google Scholar
• Goyal S. S., Huffacker R. C. The uptake of NO3, NO2, and NH14 by intact wheat (Triticum aestivum) seedlings. 1. Induction and kinetics of transport systems. Plant Physiology 1986; 82: 1051–1056
   PubMed Web of Science ®Google Scholar
• Grabov A., Böttger M. Are redox reactions involved in regulation of K+ channels in the plasma membrane of Limnobium stoloniferum root hairs?. Plant Physiology 1994; 105: 927–935
   Google Scholar
• Grabov A., Felle H., Böttger M. Modulation of the plasma membrane electron transfer system in root cells of Limnobium stoloniferum by external pH. Journal of Experimental Botany 1993; 44: 725–730
   Web of Science ®Google Scholar
• Grusack M. A., Welch R. M., Kochian L. V. Physiological characterization of a single-gene mutant of Pisum sativum exhibiting excess iron accumulation. Plant Physiology 1990; 93: 976–981
   Google Scholar
• Guerinot M. L. Iron uptake in Arabidopsis thaliana. International Conference of Bioiron (ICBI) Asheville, North Carolina 16–21 April, 1995; 2
   Google Scholar
• Guerinot M. L., Yi Y. Iron: nutrition, noxious, and not readily available. Plant Physiology 1994; 104: 815–820
   PubMed Web of Science ®Google Scholar
• Guerrini F., Valenti V., Pupillo P. Solubilization and purification of NAD(P)H dehydrogenase of Cucurbita microsomes. Plant Physiology 1987; 85: 828–834
   PubMed Web of Science ®Google Scholar
• Guerrini F., Lombini A., Bizarri M., Pupillo P. The effect of calcium chelators on microsomal pyridine nucleotide-linked dehydrogenases of sugarbeet cells. Journal of Experimental Botany 1994; 45: 1227–1233
   Google Scholar
• Hager A., Brich M. Blue-light induced phosphorylation of a plasma-membrane protein from phototropically sensitive tips of maize coleoptiles. Planta 1993; 189: 567–576
   Web of Science ®Google Scholar
• Hager A., Brich M., Bazlen I. Redox dependence of the blue-light-induced phosphorylation of a 100 kDa protein on isolated plasma membranes from tips of coleoptiles. Planta 1993; 190: 120–126
   Google Scholar
• Hassidim M., Rubinstein B., Lerner H. R., Reinhold L. Generation of a membrane potential by electron transport in plasmalemma-enriched vesicles of cotton and radish. Plant Physiology 1987; 85: 872–875
   PubMed Web of Science ®Google Scholar
• Hendry G. A. F., Houghton J. D., Jones D. T. G. The cytochromes in microsomal fractions of germinating mung beans. Biochemistry 1981; 194: 743–751
   Google Scholar
• Hilgendorf F., Böttger M. Influence of temperature on proton secretion and hexacyanoferrate (III) reduction of Zea mays L. roots. Plant Physiology 1993; 101: 1349–1353
   Google Scholar
• Hoarau J., Nasto A., Lavergne D., Flipo V., Hirel B. Nitrate reductase activity changes during a culture cycle of tobacco cells: the participation of a membrane-bound form enzyme. Plant Science 1991; 79: 193–204
   Google Scholar
• Holden M. J., Luster D. G., Chaney R. L. Enzymatic iron reduction at the root plasma membrane: Partial purification of the NADH-Fe-chelate reductase. Biochemistry of Metal Micronutrients in the Rhizosphere, J. A. Manthey, D. E. Crowley, D. G. Luster. Lewis, Boca Raton, FL 1994; 285–294
   Google Scholar
• Horemans N., Asard H., Caubergs R. J. The role of ascorbate free radical as an electron acceptor to cytochrome b-mediated trans-plasma membrane electron transport in higher plants. Plant Physiology 1994; 104: 1455–1458
   PubMed Web of Science ®Google Scholar
• Horemans N., Asard H., Caubergs R. J. Is there a carrier for vitamin C (ascorbic acid) in the plasma membrane of higher plants?. 10th International Workshop on Plant Membrane Biology. Regensburg, Germany 6–11 August, 1995, (abstract No. R26)
   Google Scholar
• Ievinch G., Valcina A., Ozola D. Induction of ascorbate peroxidase activity in stressed pine (Pinus sylvestris L.) needles: A putative role for ethylene. Plant Science 1995; 112: 167–173
   Google Scholar
• Ishimamura A., Yamazaki I. The carbon monoxide binding hemoprotein reducible by hydrogen peroxide in the microsomal fraction of pea seeds. Journal of Biological Chemistry 1977; 252: 199–204
   Google Scholar
• Ivankina N. G., Novak V. A. H'-transport across the plasmalemma. H+-ATPase or redox chain?. Plant Membrane Transport, R. M. Spanswick, W. J. Lucas, J. Dainty. Elsevier, Amsterdam 1980; 503–504
   Google Scholar
• Ivankina N. G., Novak V. A. Localization of redox reactions in plasmalemma of Elodea leaf cells. Studia Biophysica 1981; 83: 197–200
   Google Scholar
• Ivankina N. G., Novak V. A. Transplasmalemma redox reactions and ion transport in photosynthetic and heterotrophic plant cells. Physiologia Plantarum 1988; 73: 161–164
   Web of Science ®Google Scholar
• Ivankina N. G., Novak V. A., Miklashevich A. I. Redox reactions and active H' -transport in the plasmalemma of Elodea leaf cells. Membrane Transport in Plants, W. J. Cram, K. Janacek, R. Rybova, S. Sigler. John Wiley & Sons, New York 1984; 404–405
   Google Scholar
• Jacobs J. M., Jacobs N. J. Terminal enzymes of heme biosynthesis in the plant plasma membrane. Archives of Biochemistry and Biophysics 1995; 323: 274–278
   PubMed Web of Science ®Google Scholar
• Jesaitis A. J., Heners P. R., Hertel R., Briggs W. R. Characterization of membrane fraction containing a b-type cytochrome. Plant Physiology 1977; 59: 941–947
   PubMed Web of Science ®Google Scholar
• Johansson F., Olbe M., Sommarin M., Larsson C. Brij 58, a polyoxyethylene acyl ether, creates membrane vesicles of uniform sideness. A new tool to obtain inside-out (cytoplasmic side out) plasma membrane vesicles. Plant Journal 1995; 7: 165–173
   PubMed Web of Science ®Google Scholar
• Jones G. J., Morel F. M. M. Plasmalemma redox activity in the diatom Thalassiosira. Plant Physiology 1988; 87: 143–147
   PubMed Web of Science ®Google Scholar
• Kamachi K., Ameniya Y., Ogura N., Nakagawa H. Immunogold localization of nitrate reductase in spinach (Spinacea oleracea) leaves. Plant Cell Physiology 1987; 28: 333–338
   Google Scholar
• Kauss H. Some aspects of calcium-dependent regulation in plant metabolism. Annual Review of Plant Physiology 1987; 38: 47–72
   Google Scholar
• Kjellbom P., Larsson C., Askerlund P., Schelin C., Widell S. Cytochrome P-450/420 in plant plasma membranes: a possible component of the blue-light reducible flavoprotein-cytochrome complex. Photochemistry and Photobiology 1985; 42: 779–783
   Web of Science ®Google Scholar
• Klobus G., Buczek J. The role of plasma membrane oxidoreductase activity in proton transport. Journal of Plant Physiology 1995; 146: 103–107
   Web of Science ®Google Scholar
• Kneen B. E., LaRue T. A., Welch R. M., Weeden N. F. Pleiotropic effects of brz. A mutation in Pisum sativum (L.) cv. 'Sparkle' conditioning decreased nodulation, increased iron uptake and leaf necrosis. Plant Physiology 1990; 93: 717–722
   PubMedGoogle Scholar
• Krüger S. Untersuchungen zur Energetisierung plasmalem-magebundener Redoxprozesse. PhD Thesis, University Hamburg, Germany 1993
   Google Scholar
• Krüger S., Böttger M. NADH or NADPH?. Plasma Membrane Oxidoreductases in Control of Animal and Plant Growth, F. L. Crane, D. J. Morrè, H. Low. NATO ASI Series 183, A: Life Sciences, Plenum Press, New York 1988; 105–114
   Google Scholar
• Kuschel L., Dahse I., Müller E. Lack of correlation between transplasmalemma electron transport rate and depolarization in Egeria densa leaf cells. Journal of Plant Physiology 1996; 147: 675–684
   Google Scholar
• Lagendijk J., Ubbink J. B., Vermaak W. J. H. Measurement of the ratio between the reduced and oxidized forms of coenzyme Q10 in human plasma as a possible marker of oxidative stress. Journal of Lipid Research 1996; 37: 67–75
   PubMed Web of Science ®Google Scholar
• Laliberté J. F., Sun I. L., Crane F. L., Clarke M. J. Ruthenium ammine complexes as electron acceptor for growth stimulation by plasma membrane electron transport. Journal of Bioenergetics and Biomembranes 1987; 19: 69–81
   Google Scholar
• Laurie S. H., Manthey J. A. The chemistry and role of metal ion chelation in plant uptake processes. Biochemistry of Metal Micronutrients in the Rhizosphere, J. A. Manthey, D. E. Crowley, D. G. Luster. Lewis, Boca Raton, FL 1994; 165–182
   Google Scholar
• Lawrence K., Bhalla P., Misra P. C. Changes in NAD(P)H-dependent redox activities in plasmalemma-enriched vesicles isolated from boron- and zinc-deficient chick pea roots. Journal of Plant Physiology 1995; 146: 652–657
   Web of Science ®Google Scholar
• Leong T., Briggs W. R. Partial purification and characterization of a blue light-sensitive cytochrome-flavin complex from corn membrane. Plant Physiology 1981; 67: 1042–1046
   Google Scholar
• Leong T., Vierstra R. D., Briggs W. R. A blue light-sensitive cytochrome-flavin complex from corn coleoptils further characterization. Photochemistry and Photobiology 1981; 34: 697–703
   Google Scholar
• Löppert H. Energy coupling for membrane hyperpolarization in Lemna: respiration rate, ATP level and membrane potential at low oxygen concentration. Planta 1983; 159: 329–335
   Google Scholar
• Lundegårdh H. Mechanism of absorption, transport, accumulation and secretion of ions. Annual Review of Plant Physiology 1955; 6: 1–24
   Google Scholar
• Luster D. G., Buckhout T. J. Characterization and partial purification of multiple electron transport activities in plasma membranes from maize (Zea mays) roots. Physiologia Plantarum. 1988; 73: 339–347
   Google Scholar
• Luster D. G., Buckhout T. J. Purification and identification of a plasma membrane associated electron transport protein from maize (Zea mays L.) roots. Plant Physiology 1989; 91: 1014–1019
   PubMedGoogle Scholar
• Lüthen H., Böttger M. Hexachloroiridate IV as an electron acceptor for a plasmalemma redox system in maize roots. Plant Physiology 1988; 86: 1044–1047
   PubMed Web of Science ®Google Scholar
• Lüthen H., Böttger M. Induction of elongation in maize coleoptiles by hexachloroiridate and its interrelation with auxin and fusicoccin. Physiologia Plantarum 1993; 89: 77–86
   Google Scholar
• Lüthen H., Böttger M. The role of protons in the auxin-induced root growth inhibition—a critical reexamination. Botanica Acta 1993; 106: 58–63
   Google Scholar
• Lüthje S. Occurrence of a K-type vitamin in plasma membranes of maize (Zea mays L.) roots. 10th International Workshop on Plant Membrane Biology, RegensburgGermany, August, 6–11, 1995, (abstract No. V20)
   Google Scholar
• Lüthje S., Böttger M. Hexabromoiridate IV as an electron acceptor: comparison with hexachloroiridate IV and hexacyanofer-rate III. Biochimica et Biophysica Acta 1989; 977: 335–340
   Google Scholar
• Lüthje S., Böttger M. On the function of a K-type vitamin in plasma membranes of maize (Zea mays L.) roots. Mitteilungen aus dem Institut fur Allgemeine Botanik Hamburg 1995; 25: 5–13
   Google Scholar
• Lüthje S., Döring O., Böttger M. The effects of vitamin K3 and dicumarol on the plasma membrane redox system and H1 pumping activity of Zea mays L. roots measured over a long time scale. Journal of Experimental Botany 1992; 43: 183–188
   Google Scholar
• Lüthje S., GonzAles-Reyes J. A., Navas P., Döring O., Böttger M. Inhibition of maize (Zea mays L.) root plasma membrane-bound redox activities by coumarins. Zeitschrift Naturforschung 1994; 49c: 447–452
   Google Scholar
• Lüthje S., Steffen D., Busch M. A., Döring O. Plasma membrane-bound redox activities: Differences between the standard system and nitrate reductase. Fourth International Symposium on Inorganic Nitrogen Assimilation and the First Fohs Biostress Symposium, Seeheim, DarmstadtGermany, 23–28 July, 1995, (abstract No. 75)
   Google Scholar
• Lüthje S., Niecke M., Böttger M. Iron and copper in plasma membranes of maize (Zea mays L.) roots investigated by proton induced X-ray emission (PIXE). Protoplasma 1995; 184: 145–150
   Google Scholar
• Malerba M., Crosti P., Bianchetti R. Ferricyanide induced ethylene production is a plasma-membrane proton pump dependent 1-aminocyclopropane-1-carboxylic acid (ACC) oxidase activation. Journal of Plant Physiology 1995; 147: 182–190
   Google Scholar
• Marco A., deJia C., Fischer-Schliebs E., Varanini Z., Lüttge U. Evidence for two different nitrate-reducing activities at the plasma membrane in roots of Zea mays L. Planta 1994; 194: 557–564
   Google Scholar
• Marrè M. T., Moroni A., Albergoni F. G., Marre E. Plasmalemma redox activity and H1 extrusion. I. Activation of the H -pump by ferricyanide-induced potential depolarization and cytoplasm acidification. Physiologia Plantarum 1988; 87: 25–29
   Google Scholar
• Marschner H., Römheld V. Strategies of plants for acquisition of iron. Plant and Soil 1994; 165: 261–274
   Web of Science ®Google Scholar
• Mehdy M. C. Active oxygen species in plant defense against pathogens. Plant Physiology 1994; 105: 467–472
   PubMed Web of Science ®Google Scholar
• Mehlhorn H., Lelandais M., Korth H. G., Foyer C. H. Ascorbate is the natural substrate for plant peroxidases. FEBS Letters 1996; 378: 203–206
   PubMed Web of Science ®Google Scholar
• Meya G., Kowallik W. Involvement of two different photo-receptors in the light regulation of glutamine synthetase activity in a chlorophyll-free Chlorella mutant. Zeitschrift Naturforschung 1994; 49c: 757–762
   Google Scholar
• Meyerhoff P. A., Fox T. C., Travis R. L., Huffaker R. L. Characterization of the association of nitrate reductase with barley (Hordeum vulgare L.) root membranes. Plant Physiology 1994; 104: 925–936
   PubMedGoogle Scholar
• Mitchell P., Moyle J. The role of ubiquinone and plasto-quinone in chemiosmotic coupling between electron transfer and proton translocation, Q Coenzyme, G. Lenaz. Wiley & Sons, Chichester 1985; 145–163
   Google Scholar
• Miyagi N., Satho S., Fujii T. A nitrate-inducible plasma membrane protein of a marine alga, Heterosigma akashiwo. Plant Cell Physiology 1992; 33: 971–976
   Google Scholar
• Møller I. M., Askerlund P., Widell S. Electron transport constituents in the plant plasma membrane. Oxidoreduction at the Plasma Membrane: Relation to Growth and Transport, 2, Plants, F. L. Crane, D. J. Morrè, H. E. Löw. CRC Press, Boca Raton, FL 1991; 35–59
   Google Scholar
• Møller I. M., Fredlund K. M., Berczi A. The stereospeci-ficity, purification, and characterization of an NADH-ferricyanide reductase from spinach leaf plasma membrane. Protoplasma 1995; 184: 124–132
   Google Scholar
• Moog P. R., Brüggemann W. Iron reductase systems on the plant plasma membrane—a review. Plant and Soil 1994; 165: 241–260
   Web of Science ®Google Scholar
• Morré D. J. Hormone- and growth factor-stimuiated NADH oxidase. Journal of Bioenergetics and Biomembranes 1994; 26: 421–433
   PubMed Web of Science ®Google Scholar
• Morré D. J., Brightman A. O. NADH oxidase of plasma membranes. Journal of Bioenergetics and Biomembranes 1991; 23: 469–489
   PubMed Web of Science ®Google Scholar
• Morré D. J., Navas P., Penel C., Castillo F. J. Auxin-stimulated NADH oxidase (semidehydroascorbate reductase) of soybean plasma membrane: role in acidification of cytoplasm?. Protoplasma 1986; 133: 195–197
   Web of Science ®Google Scholar
• Morré D. J., Brightman A. O., Wu L. Y., Barr R., Leak B., Crane F. L. Role of plasma membrane redox activities in elongation growth in plants. Physiologia Plantarum 1988; 73: 187–193
   Web of Science ®Google Scholar
• Morré D. J., Brightman A. O., Hidalgo A., Navas P. Selective inhibition of auxin-stimulated oxidase activity and elongation growth of soybean hypocotyls by thiol reagents. Plant Physiology 1995; 107: 1285–1291
   PubMedGoogle Scholar
• Murphy T. M., Auh C. K. The superoxide synthases of plasma membrane preparations from cultured rose cells. Plant Physiology 1996; 110: 621–629
   PubMed Web of Science ®Google Scholar
• Navas P., Gomez-Diaz C. Ascorbate free radical and its role in growth control. Protoplasma 1995; 184: 8–13
   Google Scholar
• Navas P., Villalba J. M., Cordoba F. Ascorbate function at the plasma membrane. Biochimica et Biophysica Acta 1994; 1197: 1–13
   PubMed Web of Science ®Google Scholar
• Nitsch G. Redoxvorgänge an der pflanzlichen Plasmamembran. Untersuchungen in vitro an Koleoptilen von Zea mays L. PhD thesis. University Hamburg, Germany 1994
   Google Scholar
• Njus D., Kelley P. M. The secretory-vesicle ascorbate-regenerating system: a chain of concerted H1 /e -transfer reactions. Biochimica et Biophysica Acta 1993; 1144: 235–248
   PubMed Web of Science ®Google Scholar
• Novak V. A., Ivankina N. G. Nature of electrogenesis and ion transport in plant cells. Doklady Akademii Nauk SSSR 1978; 242: 1229–1232, (in Russian)
   Google Scholar
• Novak V. A., Ivankina N. G. Light induced absorption of ions by cells of freshwater plants. Fiziologia Rastenii 1978; 25: 315–322, (English translation in Soviet Plant Physiology 25, 248–254).
   Google Scholar
• Novak V. A., Ivankina N. G. Oxygen dependence of the membrane potential of photosynthetic plant cells. Citology 1978c; 20: 896–902, (in Russian)
   Google Scholar
• Otter T., Polle A. The influence of apoplastic ascorbate on the activities of cell-wall associated peroxidase and NADH oxidase in needles of norway spruce (Picea abies L.). Plant and Cell Physiology 1994; 35: 1231–1238
   Google Scholar
• Palmer J. M., Short T. W., Gallagher S., Briggs W. R. Blue light-induced phosphorylation of a plasma membrane-associated protein in Zea mays L. Plant Physiology 1993; 102: 1211–1218
   PubMed Web of Science ®Google Scholar
• Pattison S., Nelson M., Barr R., Crane F. L. The effect of diamide and buthionine sulfoximine on glutathione pools and transmembrane electron transport by cultured carrot cells. Proceedings of the Indiana Academy of Science, USA 1989; 97: 115–119
   Google Scholar
• Penel C., Castillo F. J. Peroxidases of plant plasma membranes, apoplastic ascorbate, and relation of redox activities to plant pathology. Oxidoreduction at the Plasma Membrane: Relation to Growth and Transport 2, Plants, F. L. Crane, D. J Morré, H. E. JLow. CRC Press, Boca Raton, FL 1991; 121–147
   Google Scholar
• Pinton R., Cakmak I., Marschner H. Zinc deficiency enhanced NAD(P)H dependent superoxide radical production in plasma membrane vesicles isolated from roots of bean plants. Journal of Experimental Botany 1994; 45: 45–50
   Google Scholar
• Polevoy V. V., Salamatova T. Auxin, proton pump and cell tropics. Regulation of Membrane Activities in Plants, E. Marré, O. Ciferri. Elsevier, Amsterdam 1977; 209–216
   Google Scholar
• Polle A., Wieser G., Havranek W. M. Quantification of ozone influx and apoplastic ascorbate content in needles of norway spruce trees (Picea abies L., KARST) at high altitude. Plant Cell and Environment 1995; 18: 681–688
   Web of Science ®Google Scholar
• Pönitz J., Roos W. A glucose-activated electron transfer system in the plasma membrane stimulates the H' -ATPase in. Penicillium cyclopium. Journal of Bacteriology 1994; 176: 5429–5438
   Google Scholar
• Pupillo P., Valenti V., De Luca L., Hertel R. Kinetic characterization of reduced pyridine nucleotide dehydrogenase (duroquinone-dependent) in Cucurbita microsomes. Plant Physiology 1986; 80: 384–389
   PubMedGoogle Scholar
• Qiu Q. S., Cheng P., Liang H. G. Characterization of the NAD(P)H oxidation by purified plasma membrane vesicles using a spin-trapping EPR method. Journal of Plant Physiology 1995; 146: 445–449
   Google Scholar
• Qiu Z. S., Rubinstein B., Stern A. I. Evidence for electron transport across the plasma membrane of Zea mays root cells. Planta 1985; 165: 383–391
   PubMed Web of Science ®Google Scholar
• Ramirez J. R., Gallego G., Serrano R. Electron transfer constituents in plasma membrane fractions of Avena sativa and Saccharomyces cerevisiae. Plant Science Letters 1984; 34: 103–110
   Google Scholar
• Rasmusson A. G. Effect of calcium ions and inhibitors on internal NAD(P)H dehydrogenases in plant mitochondria. European Journal of Biochemistry 1991; 202: 617–623
   Google Scholar
• Redinbaugh M. G., Campbell W. H. Reduction of ferric citrate catalyzed by NADH: nitrate reductase. Biochemical and Biophysical Research Communications 1983; 114: 1182–1188
   PubMed Web of Science ®Google Scholar
• Reichart D., Salaün J. P., Benveniste I., Durst F. Time course of induction of cytochrome P-450, NADPH-cytochrome c reductase and cinnamic acid hydroxylase by phenobarbital, ethanol, herbicides, and manganese in higher plants microsomes. Plant Physiology 1980; 66: 600–604
   Google Scholar
• Riedel J., Kunze M., Stöhr C., Tischner R. Evidence for a plasma membrane-bound nitrate reductase (PM-NR) in green tissue of higher plants. Fourth International Symposium on Inorganic Nitrogen Assimilation and the First Fohs Biostress Symposium, Seeheim, DarmstadtGermany, 23–28 July, 1995, (abstract No. 106)
   Google Scholar
• Robertson R. N. Ion transport and respiration. Biological Reviews 1960; 35: 231–255
   Web of Science ®Google Scholar
• Rodriguez-Aguilera J. C., Navarro F., Arroyo A., Alcain F. J., Villalba J. M., Navas P. Vitamin C stabilization as a consequence of the plasma membrane redox system. Protoplasma 1995; 184: 229–232
   Google Scholar
• Römheld V., Marschner H. Mechanism of iron uptake by peanut plants. I. Fe III reduction, chelate splitting, and release of phenolics. Plant Physiology 1983; 71: 949–954
   PubMed Web of Science ®Google Scholar
• Rubinstein B., Luster D. G. Plasma membrane redox activity: components and role in plant processes. Annual Reviews in Plant Physiology and Molecular Biology 1993; 44: 131–155
   Web of Science ®Google Scholar
• Rubinstein B., Stern A. I. Relationship of transplasmalemma redox activity to proton and solute transport by roots of Zea mays. Plant Physiology 1986; 80: 805–811
   PubMed Web of Science ®Google Scholar
• Rubinstein B., Stern A. I. Proton release and plasmalemma redox in plants. Oxidoreduction at the Plasma Membrane: Relation to Growth and Transport, 2, Plants, F. L. Crane, D. J. Morré, H. E. Löw. CRC Press, Boston, MA 1991; 167–187
   Google Scholar
• Rubinstein B., Stern A. I. The role of plasma membrane redox activity in light effects in plants. Journal of Bioenergetics and Biomembranes 1991; 23: 393–408
   Google Scholar
• Rubinstein B., Stern A. I., Stout R. G. Redox activity at the surface of oat root cells. Plant Physiology 1984; 76: 386–391
   PubMed Web of Science ®Google Scholar
• Ruyters G. Effects of blue light on enzymes. Blue Light Effects in Biological Systems, H. Senger. Springer, Berlin 1984; 283–301
   Google Scholar
• Salguero J., Böttger M. Secreted catalase activity in roots of developing maize (Zea mays L.) seedlings. Protoplasma 1995; 184: 72–78
   Google Scholar
• Sandelius A. S., Barr R., Crane F. L., Morré D. J. Redox reactions of plasma membranes isolated from soybean hypocotyls by phase partition. Plant Science 1986; 48: 1–10
   Web of Science ®Google Scholar
• Santos-Ocana C., Navas P., Crane F. L., Cordoba F. Extracellular ascorbate stabilization as a result of trans plasma membrane electron transfer in Saccharomyces cerevisiae. Journal of Bioenergetics and Biomembranes 1995; 27: 597–603
   Google Scholar
• Schmidt W. Root-mediated ferric reduction—responses to iron deficiency, exogenously induced changes in hormonal balance and inhibition of protein synthesis. Journal of Experimental Botany 1994; 45: 725–731
   Google Scholar
• Schmidt W., Butler W. L. Flavin mediated photoreactions in artificial systems: a possible model for the blue light photoreceptor pigment in living cells. Photochemistry and Photobiology 1976; 24: 71–75
   Google Scholar
• Schmieden U., Wild A. Changes in levels of ã-tocopherol and ascorbate in spruce needles at three low mountain sites exposed to Mg2 -deficiency and ozone. Zeitschrift für Naturforschung 1994; 49c: 171–180
   Google Scholar
• Schweinzer E., Mao Y., Krajnik P., Getoff N., Goldenberg H. Reduction of extracellular dehydroascorbic acid by K562 cells. Cell Biochemistry and Function 1996; 14: 27–31
   PubMed Web of Science ®Google Scholar
• Segal A. W. The NADPH oxidase of phagocytic cells is an electron pump that alkalinizes the phagocytic vacuole. Protoplasma 1995; 184: 86–103
   Google Scholar
• Seidenberg S., Döring O., Krüger S., Lüthje S., Böttger M. Changes in the glutathione level induced by trans-plasma membrane electron transport in maize (Zea mays L.). Protoplasma 1995; 184: 238–248
   Google Scholar
• Serrano A., Cordoba F., Gonzales-Reyes J. A., Navas P., Villalba J. M. Purification and characterization of two distinct NAD(P)H dehydrogenases from onion (Allium cepa L.) root plasma membrane. Plant Physiology 1994; 106: 87–96
   Google Scholar
• Serrano A., Cordoba F., Gonzalez-Reyes J. A., Santos C., Navas P., Villalba J. M. NADH-specific dehydrogenase from onion root plasma membrane: purification and characterization. Protoplasma 1995; 184: 133–139
   Google Scholar
• Serrano R. Structure and function of plasma membrane ATPases. Annual Reviews in Plant Physiology and Plant Molecular Biology 1989; 40: 61–94
   Web of Science ®Google Scholar
• Short T. W., Porst M., Briggs W. R. A photoreceptor system regulating in vivo and in vitro phosphorylation of a pea plasma membrane protein. Photochemistry and Photobiology 1992; 55: 773–781
   Google Scholar
• Siebrecht S., Mack G., Tischner R. Function and contribution of the root tip in the induction of NO3-uptake along the barley root axis. Journal of Experimental Botany 1995; 46: 1669–1676
   Web of Science ®Google Scholar
• Sijmons P. C., Bienfait H. F. Source of electrons for extracellular Fe(III) reduction in iron-deficient bean roots. Physiologia Plantarum 1983; 59: 409–415
   Web of Science ®Google Scholar
• Sijmons P. C., Lanfermeijer F. C., DeBoer A. H., Prins H. B. A., Bienfait H. F. Depolarization of cell membrane potential during trans-plasma membrane electron transfer to extracellular electron acceptors in iron-deficient roots of Phaseolus vulgaris L. Plant Physiology 1984; 76: 943–946
   PubMed Web of Science ®Google Scholar
• Sijmons P. C., van denBriel W., Bienfait H. F. Cytosolic NADPH is the electron donor for extracellular Fell reduction in iron-deficient bean roots. Plant Physiology 1984; 75: 219–221
   PubMed Web of Science ®Google Scholar
• Sijmons P. C., Lanfermeijer F. C., Bienfait F. Root NAD(P)H levels in monocotyledonous species differing in their response to iron-deficiency. Plant Physiology Supplement 1984c; 75, No. 1083.
   Google Scholar
• Slayman C. L. Movement of ions and electrogenesis in microorganisms. American Zoology 1970; 10: 377–392
   Google Scholar
• Smarelli J., Campbell W. H. NADH dehydrogenases activity of higher plant nitrate reductase (NADH). Plant Science Letters 1979; 16: 139–147
   Google Scholar
• Solomonson L. P., Barber M. J. Assimilatory nitrate reductase: functional properties and regulation. Annual Review in Plant Physiology and Molecular Biology 1990; 41: 225–253
   Web of Science ®Google Scholar
• Spring O., Wolz C., Hager A. Auxin induced N-ethylma-leimide (NEM) effects on elongation growth of coleoptiles and auxin-induced (14C)-NEM labeling of membrane proteins. Physiologia Plantarum 1988; 72: 305–310
   Google Scholar
• Stöhr C., Tischner R., Ward M. K. Characterization of the plasma-membrane-bound nitrate reductase in Chlorella saccharophila (Krüger) Nadson. Planta 1993; 191: 79–85
   Google Scholar
• Stöhr C., Glogau U., Matschke M., Tischner R. Evidence for the involvement of plasma-membrane-bound nitrate reductase in signal transduction during blue-light stimulation of nitrate uptake in Chlorella saccharophila. Planta 1995; 197: 613–618
   Google Scholar
• Stöhr C., Schuler F., Tischner R. Glycosyl-phosphati-dylinositol-anchored proteins exist in the plasma membrane of Chlorella saccharophila (Krüger) Nadson: Plasma membrane-bound nitrate reductase as an example. Planta 1995; 196: 284–287
   Google Scholar
• Struglics A., Fredlund K. M., Rasmusson A. G., Møller I. M. The presence of a short redox chain in the membrane of intact potato tuber peroxisomes and the association of malate dehydrogenase with the peroxisomal membrane. Physiologia Plantarum 1993; 88: 19–28
   Google Scholar
• Susin S., Abadia A., González-Reyes J. A., Lucena J. J., Abadia J. The pH requirements for in vivo activity of the iron-deficiency-induced 'turbo' ferric chelate reductase. Plant Physiology 1996; 110: 111–123
   PubMed Web of Science ®Google Scholar
• Sutherland M. W. The generation of oxygen radicals during host plant responses to infection. Physiological and Molecular Plant Pathology 1991; 39: 79–93
   Web of Science ®Google Scholar
• Szabo-Nagy A., Erdei L. The effects of iron deficiency on the ATPase and ferricyanide reductase activities of plasma membrane purified by phase partitioning from sunflower roots. Journal of Plant Physiology 1993; 142: 579–584
   Google Scholar
• Takahama U. Redox state of ascorbic acid in the apoplast of stems of Kalanchoe daigremontiana. Physiologia Plantarum 1993; 89: 791–798
   Web of Science ®Google Scholar
• Takeuchi Y., Kubo H., Kasahara H., Sakaki T. Adaptive alterations in the activities of scavengers of active oxygen in cucumber cotyledons irradiated with UV-B. Journal of Plant Physiology 1996; 147: 589–592
   Web of Science ®Google Scholar
• Tanaka O., Cleland C. F. Comparison of the ability of salicylic acid and ferricyanide to induce flowering in the long-day plant, Lemna gibba G3. Plant Physiology 1980; 65: 1058–1061
   Google Scholar
• Taylor A., Assmann S. Electrophysiological study of blue light-modulated plasma membrane pump current in guard cells of Vicia faba. 10th International Workshop on Plant Membrane Biology, RegensburgGermany, 6–11 August, 1995, (abstract No. S14)
   Google Scholar
• Thibaud J. B., Romieu C., Gibrat R., Grouzis J. P., Grignon C. Local ionic environment of plant membranes: effects on membrane functions. Zeitschrift für Pflanzenphysiologie 1984; 114: 207–213
   Google Scholar
• Tischner R., Ward M. R., Huffaker R. C. Evidence for a plasma-membrane-bound nitrate reductase involved in nitrate uptake of Chlorella sorokiniana. Planta 1989; 178: 19–24
   PubMed Web of Science ®Google Scholar
• Tischner R., Waldeck B., Goyal S. S., Rains W. D. 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 1993; 189: 533–537
   Web of Science ®Google Scholar
• Trockner V., Marré E. Plasmalemma redox chain and H' extrusion. II. respiratory and metabolic changes associated with fusicoccin-induced and with ferricyanide-induced H' extrusion. Plant Physiology 1988; 87: 30–35
   PubMed Web of Science ®Google Scholar
• Trost P., Bonora P., Scagliarini S., Pupillo P. Purification and properties of NAD(P)H:(quinone-acceptor) oxidoreductase of sugarbeet cells. European Journal of Biochemistry 1995; 234: 452–548
   Google Scholar
• Ullrich C. I., Köhler K., Baier M., Förster B., Hartung W. Neutral red as a redox dye induces K' efflux and current-voltage changes in Eremosphaera, Lemna and guard cells. Botanica Acta 1990; 103: 214–221
   Google Scholar
• Valenti V., Minardi P., Guerrini F., Mazzucchi U., Pupillo P. Increase of plasma membrane NADH-duroquinone reductase in tobacco leaves treated with protein-lipopolysaccharide complexes. Plant Physiology and Biochemistry 1989; 27: 569–576
   Google Scholar
• Vianello A., Macri F. Generation of superoxide anion and hydrogen peroxide at the surface of plant cells. Journal of Bioenergetics and Biomembranes 1991; 23: 409–423
   PubMedGoogle Scholar
• Ward M. R., Tischner R., Huffaker R. C. Inhibition of nitrate transport by anti-nitrate reductase lgG fragments and the identification of plasma membrane associated nitrate reductase in roots of barley seedlings. Plant Physiology 1988; 88: 1141–1145
   PubMedGoogle Scholar
• Welch R. M., LaRue T. A. Physiological characteristics of Fe accumulation in the 'bronze' mutant of Pisum sativum L., cv 'Sparkle' E107 (brz brz). Plant Physiology 1990; 93: 723–729
   PubMed Web of Science ®Google Scholar
• Welch R. M., Webb M. J., Loneragan J. F. Zinc in membrane function and its role in phosphorous toxicity. Proceedings of 9th International Plant Nutrition Colloquium, A. Scaife. Commonwealth Agricultural Bureau, Farham Royal Bucks 1982; 711–715
   Google Scholar
• Widell S. Membrane-bound blue light receptors—possible connection to blue light photomorphogenesis. Blue Light Responses: Phenomena and Occurrence in Plants and Microorganisms, H. Senger. CRC Press, Boston, MA 1987; 2: 89–98
   Google Scholar
• Widell S., Larsson C. Distribution of cytochrome b photo-reduction by endogenous photosensitizer or methylene blue in fractions from corn and cauliflower. Physiologia Plantarum 1983; 57: 196–202
   Google Scholar
• vonWiren N., Marschner H., Römheld V. Uptake of Zn-phytosiderophores in maize. 10th International Workshop on Plant Membrane Biology, RegensburgGermany, 6–11 August, 1995, (abstract No. R43)
   Google Scholar
• Xu J. X., King T. E. Two-site property of thenoyltri-fluoroacetone inhibiting succinate-ubiquinone reductase. Science China Series. B—Chemistry in Life Science and Earth 1992; 35: 162–168
   Google Scholar
• Yamaguchi H., Fujiwara T., Mori S. Genetic introduction of the gene coding yeast ferric reductase into tobacco plants. International Conference of Bioiron (ICBI). Asheville, North Carolina 16–21 April, 1995; 84
   Google Scholar
• Yi Y., Saleeba J. A., Guerinot M. L. Iron uptake in Arabidopsis thaliana. Biochemistry of Metal Micronutrients in the Rhizosphere, J. A. Manthey, D. E. Crowley, D. G. Luster. Lewis, Boca Raton, FL 1994; 295–307
   Google Scholar
• Yuan D. S., Steaman R., Dancis A., Dunn A., Buler T., Klaussner R. D. The Menk/Wilson diseases gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake. Proceedings of the National Academy of Sciences, USA 1995; 92: 2632–2636
   PubMed Web of Science ®Google Scholar
• Zaharieva T., Yamashita K., Matsumoto H. Changes in ascorbate metabolism in iron deficient cucumber plants. International Conference of Bioiron (ICBI). Asheville, North Carolina 16–21 April, 1995; 168
   Google Scholar
• Zhao S., Colombo S. J., Blumwald E. The induction of freezing tolerance in jack pine seedlings: The role of root plasma membrane H'-ATPase and redox activities. Physiologia Plantarum 1995; 93: 55–60
   Google Scholar
• Zimmerman U. Electrical breakdown, electropermeabilization and electrofusion. Reviews in Physiological Biochemistry and Pharmacology 1986; 105: 175–256
   Google Scholar