1887

Abstract

Some kinetic properties of ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase from , a marine, facultatively heterotrophic, sulphur-oxidizing bacterium and putative symbiont of (Montagu), a bivalve mussel, have been determined. The kinetic parameters for the CO/Mg-activated enzyme were: (RuBP) 24·3 μ, (CO) 125·5 μ, K(O) 900 μ and (Mg) 1·53 m. The low CO affinity suggests that T. thyasiris may possess a CO-concentrating mechanism. RuBP oxygenase activity was inhibited by increasing CO concentration. Divalent metal ions were essential for RuBP carboxylase activity; activity of the Mg-free enzyme could be restored by the addition of Mg, Mn or Ca. The pH optimum was 7·8. The temperature optimum for RuBP carboxylase activity was 55 °C, although the enzyme rapidly lost activity at this temperature. An Arrhenius plot was biphasic, with a break at 40 °C. The activation energies were 55·5 × 10 J mol and 32·9 × 10 J mol over the temperature ranges 10–40 °C and 40–55 °C, respectively. was 2·12 for any 10 °C increment between 10·40 °C, and 1·47 between 40·55 °C. RuBP carboxylase activity was stable at 35 °C, the optimum growth temperature of . and at 7·5 °C, the temperature of the habitat of Thyasira flexuosa, but the activity was 40% and 3·5%, respectively, of the potential activity at 55 °C. RuBP carboxylase activity was stimulated by NaCl concentrations of up to 0·3 , with a maximum (33 %), occurring between 0·1 and 0·2 -NaCl. At higher concentrations of NaG (>0·3 ) RuBP carboxylase activity was inhibited

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1991-07-01
2021-04-21
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References

  1. Badger M. R. 1980; Kinetic properties of ribulose 1,5-bisphosphate carboxylase/oxygenase from Anabaena variabilis . Archives of Biochemistry and Biophysics 201:247–254
    [Google Scholar]
  2. Bowien B. 1977; dRibulose 1,5-bisphosphate carboxylase from Paracoccus denitrificans . FEMS Microbiology Letters 2:263–266
    [Google Scholar]
  3. Bradford M. M. 1976; A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72:248–254
    [Google Scholar]
  4. Buch K. 1960; Dissoziation der kohlensaure, gleichgewichte und puffersysteme. In Handbuch der Pflanzenphysiologie 11–11 Ruhland W. Berlin: Springer-Verlag;
    [Google Scholar]
  5. Cavanaugh C. M. 1985; Symbioses of chemoautotrophic bacteria and marine invertebrates from hydrothermal vents and reducing sediments. Bulletin of the Biological Society of Washington 6:373–388
    [Google Scholar]
  6. Charles A. M., White B. 1976a; Ribulose bisphosphate carboxylase from Thiobacillus A2. Its purification and properties. Archives of Microbiology 108:195–202
    [Google Scholar]
  7. Charles A. M., White B. 1976b; Physical properties and metabolite regulation of ribulose bisphosphate carboxylase from Thiobacillus A2. Archives of Microbiology 108:203–209
    [Google Scholar]
  8. Fisher M. R., Hand S. C. 1984; Chemoautotrophic symbionts in the bivalve Lucina floridarta from seagrass beds. Biological Bulletin 167:445–459
    [Google Scholar]
  9. Fisher C. R., Childress J. J., Minnich E. 1989; Autotrophic carbon fixation by the chemoautotrophic symbionts of Riftia pachyptila . Biological Bulletin 177:372–385
    [Google Scholar]
  10. Ford T. W. 1979; Ribulose 1,5-bisphosphate carboxylase from the thermophilic, acidophilic alga, Cyanidium caldarium (Geitler). Purification, characterisation and thermostability of the enzyme. Biochimica et Biophysica Acta 569:239–248
    [Google Scholar]
  11. Goldthwaite J. J., Bogorad L. 1971; A one-step method for the isolation and determination of leaf ribulose-1,5-diphosphate carboxylase. Analytical Biochemistry 41:57–66
    [Google Scholar]
  12. Heda G. D., Madigan M. T. 1988; Thermal properties and oxygenase activity of ribulose-1,5-bisphosphate carboxylase from the thermophilic purple bacterium, Chromatium tepidum . FEMS Microbiology Letters 51:45–50
    [Google Scholar]
  13. Jordan D. B., Ogren W. L. 1981; Species variation in the specificity of ribulose bisphosphate car boxy lase/oxygenase. Nature London: 291513–515
    [Google Scholar]
  14. Jordan D. B., Ogren W. L. 1983; Species variation in kinetic properties of ribulose 1,5-bisphosphate carboxylase/oxygenase. Archives of Biochemistry and Biophysics 227:425–433
    [Google Scholar]
  15. Laing W. A., Ogren W. L., Hageman R. H. 1974; Regulation of soybean net photosynthetic CO2 fixation by the interaction of CO2 O2 and ribulose 1,5-bisphosphate carboxylase. Plant Physiology 54:678–685
    [Google Scholar]
  16. McCarthy J. T., Charles A. M. 1975; Properties and regulation of ribulose diphosphate carboxylase from Thiobacillus novellus . Archives of Microbiology 105:51–59
    [Google Scholar]
  17. Miziorko H. M., & Lorimer G. H. 1983; Ribulose-1,5-bisphosphate carboxylase-oxygenase. Annual Review of Biochemistry 52:507–535
    [Google Scholar]
  18. Pierce J., McCurry S. D., Mulligan R. M., Tolbert N. E. 1982; Activation and assay of ribulose-1,5-bisphosphate carboxylase/oxygenase. In Methods in Enzymology 8947–55 Wood W. A. New York: Academic Press;
    [Google Scholar]
  19. Snead R. M., Shively J. M. 1978; dRibulose-1,5-bisphosphate carboxylase from Thiobacillus neapolitanus . Current Microbiology 1:309–314
    [Google Scholar]
  20. Southward E. C. 1986; Gill symbionts in thyasirids and other bivalve molluscs. Journal of the Marine Biological Association of the United Kingdom 66:889–914
    [Google Scholar]
  21. Southward E. C. 1987; Contribution of symbiotic chemoautotrophs to the nutrition of benthic invertebrates. In Microbes in the Sea83–118 Sleigh M. A. Chichester: Ellis Horwood;
    [Google Scholar]
  22. Southward A. J., Southward E. C. 1988; Pogonophora: Tubeworms dependent on endosymbiotic bacteria. Animal and Plant Sciences 1:203–207
    [Google Scholar]
  23. Tabita F. R., McFadden B. A. 1976; Molecular and catalytic properties of ribulose 1,5-bisphosphate carboxylase from the photosynthetic extreme halophile Ectothiorhodospira halophila . Journal of Bacteriology 126:1271–1277
    [Google Scholar]
  24. Takabe T., Rai A. N., Akazawa T. 1984; Interaction of constituent subunits in ribulose 1,5-bisphosphate carboxylase from Aphanothece halophytica . Archives of Biochemistry and Biophysics 229:202–211
    [Google Scholar]
  25. Truesdale G. A., Downing A. L., Lowden G. F. 1955; The solubility of oxygen in pure water and seawater. Journal of Applied Chemistry 5:53–62
    [Google Scholar]
  26. Warr S. R. C., Reed R. H., Stewart W. D. P. 1984; Osmotic adjustment of cyanobacteria: the effects of NaCl, KC1, sucrose and glycine betaine on glutamine synthetase activity in a marine and halotolerant strain. Journal of General Microbiology 130:2169–2175
    [Google Scholar]
  27. Weber D. J., Andersen W. R., Hess S., Hansen D. J., Gunasekaran M. 1977; Ribulose-1,5-bisphosphate carboxylase from plants adapted to extreme environments. Plant and Cell Physiology 18:693–699
    [Google Scholar]
  28. Williams C. A., Nelson D. C., Farah B. A., Jannasch H. W., Shively J. M. 1988; Ribulose bisphosphate carboxylase of the procaryotic symbiont of a hydrothermal vent tube-worm: kinetics, activity and gene hybridization. FEMS Microbiology Letters 50:107–112
    [Google Scholar]
  29. Wood A. P., Kelly D. P. 1989; Isolation and physiological characterisation of Thiobacillus thyasiris sp. nov., a novel marine facultative autotroph and the putative symbiont of Thyasiraflexuosa . Archives of Microbiology 152:160–166
    [Google Scholar]
  30. Yeoh H.-H., Badger M. R., Watson L. 1981; Variations in kinetic properties of ribulose-1,5-bisphosphate carboxylases among plants. Plant Physiology 67:1151–1155
    [Google Scholar]
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