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Changes in sugar beet leaf plasma membrane Fe(III)-chelate reductase activities mediated by Fe-deficiency, assay buffer composition, anaerobiosis and the presence of flavins

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Summary

Different assay conditions induce changes in the ferric chelate reductase activities of leaf plasma membrane preparations from Fe-deficient and Fe-sufficient sugar beet. With an apoplasttype assay medium the ferric chelate reductase activities did not change significantly when Fe(III)-EDTA was the substrate. However, with ferric citrate as substrate, the effect depended on the citrateto-Fe ratio. When the citrate-to-Fe ratio was 20 ∶ 1, the effects were practically unappreciable. However, with a lower citrate-to-Fe ratio of 5 ∶ 1 the activities were significantly lower with the apoplast-type medium than with the standard assay medium. Our data also indicate that anaerobiosis during the assay facilitates the reduction of ferric malate and Fe(III)-EDTA by plasma membrane preparations. Anaerobiosis increased by approximately 50% the plasma membrane ferric chelate reductase activities when Fe(III)-EDTA was the substrate. With ferric malate anaerobiosis increased activities by 70–90% over the values obtained in aerobic conditions. However, with ferric citrate the increase in activity by anaerobiosis was not significant. We have also tested the effect of riboflavin, flavin adenine dinucleotide, and flavin mononucleotide on the plasma membrane ferric chelate reductase activities. The presence of flavins generally increased activities in plasma membrane preparations from control and Fe-deficient plants. Increases in activity were generally moderate (lower than twofold). These increases occurred with Fe(III)-EDTA and Fe(III)-citrate as substrates.

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Abbreviations

BPDS:

bathophenantroline disulfonate

FC:

ferric chelate

FC-R:

ferric chelate reductase

PM:

plasma membrane

References

  • Abadía J (1992) Leaf responses to Fe deficiency: a review. J Plant Nutr 15: 1699–1713

    Google Scholar 

  • Bagnaresi P, Pupillo P (1995) Characterization of NADH-dependent Fe3+-chelate reductases of maize root. J Exp Bot 46: 1497–1503

    Google Scholar 

  • —, Basso B, Pupillo P (1997) The NADH-dependent Fe3+-chelate reductases of tomato roots. Planta 202: 427–434

    Google Scholar 

  • Belkhodja R, Morales F, Quílez R, López-Millán AF, Abadía A, Abadía J (1998) Iron deficiency causes changes in chlorophyll fluorescence due to the reduction in the dark of the photosystem II acceptor side. Photosynth Res 56: 265–276

    Google Scholar 

  • Bérczi A, Møller IM (1998) NADH-monodehydroascorbate oxidoreductase is one of the redox enzymes in spinach leaf plasma membranes. Plant Physiol 116: 1029–1036

    Google Scholar 

  • —, Fredlund KM, Møller IM (1995) Purification and characterization of the NADH-hexacyanoferrate(III) reductase from spinach leaf plasma membrane. Arch Biochem Biophys 320: 65–72

    Google Scholar 

  • Bienfait HF (1985) Regulated redox processes at the plasmalemma of plant root cells and their function in iron uptake. J Bioenerg Biomembr 17: 73–83

    Google Scholar 

  • — (1988) Mechanisms in Fe-efficiency reactions of higher plants. J Plant Nutr 11: 605–629

    Google Scholar 

  • —, Bino RJ, van der Bliek AM, Duivenboorden JF, Fontaine JM (1983) Characterization of ferric reducing activity in roots of FedeficientPhaseolus vulgaris. Physiol Plant 59: 196–202

    Google Scholar 

  • Brüggemann W, Moog PR (1989) NADH-dependent Fe3+ EDTA and oxygen reduction by plasma membrane vesicles from barley roots. Physiol Plant 75: 245–254

    Google Scholar 

  • — —, Nakagawa H, Janiesch P, Kuiper PJC (1990) Plasma membrane-bound NADH Fe3+ EDTA reductase and iron deficiency in tomato (Lycopersicon esculentum): is there a Turbo reductase? Physiol Plant 79: 339–346

    Google Scholar 

  • —, Maas-Kantel K, Moog PR (1993) Iron uptake by leaf mesophyll cells: the role of the plasma membrane-bound ferric-chelate reductase. Planta 190: 151–155

    Google Scholar 

  • Cakmak I, Van de Wetering DAM, Marschner H, Bienfait HF (1987) Involvement of superoxide radical in extracellular ferric reduction by iron-deficient bean roots. Plant Physiol 85: 310–314

    Google Scholar 

  • Chaney RL, Brown JC, Tiffin LO (1972) Obligatory reduction of ferric chelates in iron uptake by soybean. Plant Physiol 50: 208–213

    Google Scholar 

  • de la Guardia MD, Alcántara E (1996) Ferric chelate reduction by sunflower (Helianthus annuus L.) leaves: influence of light, oxygen, iron deficiency and leaf age. J Exp Bot 47: 669–675

    Google Scholar 

  • Herbik A, Giritch A, Horstmann C, Becker R, Balzer H-J, Baumlein H, Stephan U (1996) Iron and copper nutrition-dependent changes in protein expression in a tomato wild type and the nicotianamine-free mutant chloronerva. Plant Physiol 111: 533–540

    Google Scholar 

  • Holden MJ, Luster DG, Chaney RL, Buckhout TJ, Robinson C (1991) Fe3+-chelate reductase activity of plasma membranes isolated from tomato (Lycopersicon esculentum Mill.) roots: comparison of enzymes from Fe-deficient and Fe-sufficient roots. Plant Physiol 97: 537–544

    Google Scholar 

  • Hossain MW, Asada K (1985) Monodehydroascorbate reductase from cucumber is a flavin adenine dinucleotide enzyme. J Biol Chem 260: 12920–12926

    Google Scholar 

  • Jesaitis AJ, Heners PR, Hertel R, Briggs WR (1977) Characterization of a membrane fraction containing a b-type cytochrome. Plant Physiol 59: 941–947

    Google Scholar 

  • Larsson C (1985) Plasma membranes. In: Linskens H, Jackson J (eds) Cell components. Springer, Berlin Heidelberg New York Tokyo, pp 85–104 (Modern methods of plant analysis, vol 1)

    Google Scholar 

  • Markwell M, Haas SM, Tolbert NE, Lieber LL (1981) Protein determination in membrane and lipoprotein samples: manual and automated procedures. Methods Enzymol 72: 296–303

    Google Scholar 

  • Marschner H, Römheld V (1994) Strategies of plants for acquisition of iron. Plant Soil 165: 261–274

    Google Scholar 

  • — —, Kisell M (1986) Different strategies in higher plants in mobilization and uptake of iron. J Plant Nutr 9: 695–713

    Google Scholar 

  • Moog PR, Brüggemann W (1994) Iron reductase systems in the plant plasma membrane: a review. Plant Soil 165: 241–260

    Google Scholar 

  • Palmgren MG, Askerlund P, Fredrikson K, Widell S, Sommarin M, Larsson C (1990) Sealed inside-out and right-side-out plasma membrane vesicles: optimal conditions for formation and separation. Plant Physiol 92: 871–880

    Google Scholar 

  • Rabotti G, Zocchi G (1994) Plasma membrane-bound H+ ATPase and reductase activities in Fe-deficient cucumber roots. Physiol Plant 90: 779–785

    Google Scholar 

  • Rubinstein B, Luster DG (1993) Plasma membrane redox activity: components and role in plant processes. Annu Rev Plant Physiol Plant Mol Biol 44: 131–155

    Google Scholar 

  • Serrano A, Córdoba F, González-Reyes JA, Navas P, Villalba JM (1994) Purification and characterization of two distinct NAD(P)H dehydrogenases from onion (Allium cepa L.) root plasma membrane. Plant Physiol 106: 87–96

    Google Scholar 

  • Shelton P, Barton LL (1997) Ferric-citrate reductase activity inLaccaria luccata, an ectomycorrhizal fungus. In: Ninth International Symposium on Iron Nutrition and Interactions, Stuttgart, Federal Republic of Germany, Abstract Book, abstract S3-3, p 24

  • Susín S (1994) Respuestas inducidas por la deficiencia de hierro en el sistema radicular deBeta vulgaris L. PhD thesis, Universidad de Zaragoza, Zaragoza, Spain

    Google Scholar 

  • —, Abián J, Sánchez-Baeza J, Peleato ML, Abadía A, Gelpí E, Abadía J (1993a) Riboflavin 3′- and 5′-sulfate: two novel flavins accumulating in the roots of iron deficient sugar beet (Beta vulgaris L.). J Biol Chem 268: 20958–20965

    Google Scholar 

  • - Quílez R, Abadía A, Abadía J (1993b) Differences in flavin content of leaves from iron deficient and iron sufficient sugar beet (Beta vulgaris L.). In: Seventh International Symposium on Iron Nutrition and Interactions, Zaragoza, Spain, Abstract Book, abstract V-23, p 107

  • —, Abián J, Peleato ML, Sánchez-Baeza J, Abadía A, Gelpí E, Abadía J (1994) Flavin excretion from iron deficient sugar beet (Beta vulgaris L.). Planta 193: 514–519

    Google Scholar 

  • —, Abadía A, González-Reyes JA, Lucena JJ, Abadía J (1996) The pH requirement for in vivo expression of the Fe-deficiencyinduced “turbo” ferric chelate reductase: a comparison of the Fe deficiency-induced Fe reductase activities of intact plants and isolated plasma membrane fractions in sugar beet (Beta vulgaris L.). Plant Physiol 110: 111–123

    Google Scholar 

  • Tiffin LO (1966a) Iron translocation I: plant culture, exudate sampling, iron citrate analysis. Plant Physiol 41: 510–514

    Google Scholar 

  • — (1966b) Iron translocation II: citrate/iron ratios in plant stem exudates. Plant Physiol 41: 515–518

    Google Scholar 

  • Welkie GW, Miller GW (1993) Plant iron uptake physiology by nonsiderophore systems. In: Barton LL, Hemming BC (eds) Iron chelation in plants and soil microorganisms. Academic Press, San Diego, pp 345–369

    Google Scholar 

  • Widell S, Larsson C (1990) A critical evaluation of markers used in plasma membrane purification. In: Larsson C, Møller IM (eds) The plant plasma membranes: structure, function, and molecular biology. Springer, Berlin Heidelberg New York Tokyo, pp 16–43

    Google Scholar 

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González-Vallejo, E.B., Susín, S., Abadía, A. et al. Changes in sugar beet leaf plasma membrane Fe(III)-chelate reductase activities mediated by Fe-deficiency, assay buffer composition, anaerobiosis and the presence of flavins. Protoplasma 205, 163–168 (1998). https://doi.org/10.1007/BF01279306

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