1887

Abstract

Formate stimulated growth of the microaerophilic bacterium subsp. at reduced dissolved oxygen tensions (d.o.t). At a d.o.t. of 2 kPa the mean doubling time of growing in a complex medium supplemented with formate was 2 h. Growth did not occur in the absence of O. When was cultured in a complex medium with formate, growth and formate consumption slowed down after a rise of the d.o.t. from 2 to 15 kPa. At the same time the potential respiration rate diminished greatly. The effects of exposure to a d.o.t. of 15 kPa could still be reversed after 4 h by shifting the d.o.t. back to 2 kPa. The decrease in the potential respiration rate could be related to a loss of formate dehydrogenase activity. Its susceptibility to a high d.o.t. was greater when formate was present in the growth medium than in its absence. Formate oxidase had a low affinity for O and HO was a product of the oxidation of formate by O. Formate dehydrogenase appeared to be a membrane-bound enzyme. Of the possible physiological electron acceptors tested, only FAD gave rise to a detectable, although low, activity of formate dehydrogenase. grown in the complex medium with formate contained cytochromes of the - and -type. Cytochrome was membrane-bound; cytochrome was largely recovered in the soluble fraction. A CO-binding pigment was identified as a cytochrome of the -type. possessed cytochrome peroxidase activity. Cytochrome oxidases of a known type could not be detected unequivocally in a (reduced-plus-CO reduced) difference spectrum. An important role in the microaerophilic nature of is ascribed to HO.

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1980-06-01
2024-03-29
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References

  1. Bartsch R. G. 1967; Spectroscopic properties of purified cytochromes of photosynthetic bacteria. . In Bacterial Photosynthesis pp. 475–494 Gest H., Vernon L.P, San Pietro A. Edited by Antioch, Ohio: Antioch Press;
    [Google Scholar]
  2. Ellfolk N., Soininen R. 1970; Pseudomonas cytochrome c peroxidase. I. Purification procedure.. Acta chemica scandinavica 24:2126–2136
    [Google Scholar]
  3. Hoffman P. S., Krieg N. R., Smibert R. M. 1979; Studies of the microaerophilic nature of Campylobacter fetus subsp.jejuni. I. Physiological aspects of enhanced aerotolerance.. Canadian Journal of Microbiology 25:1–7
    [Google Scholar]
  4. Jacobs N. J., Wolin M. J. 1963; Electron transport system of Vibrio succinogenes. II. Inhibition of electron transport by 2-heptyI-4-hydroxyquino- line N-oxide.. Biochimica et biophysica acta 69:29–39
    [Google Scholar]
  5. Jurtshuk P. Jr Mueller T. J., Acord W. C. 1975; Bacterial terminal oxidases.. CRC Critical Reviews in Microbiology 3:399–468
    [Google Scholar]
  6. Kroger A., Innerhofer A. 1976; The function of the b cytochromes in the electron transport from formate to fumarate of Vibrio succinogenes. . European Journal of Biochemistry 69:497–506
    [Google Scholar]
  7. Laanbroek H. J., Stal L. J., Veldkamp H. 1978; Utilization of hydrogen and formate by Campylobacter spec, under aerobic and anaerobic conditions.. Archives of Microbiology 119:99–102
    [Google Scholar]
  8. Lang E., Lang H. 1972; Spezifische Farbreaktion zum direkten Nachweis der Ameisensäure.. Zeitschrift für analytische Chemie 260:8–10
    [Google Scholar]
  9. Lecce J. G. 1958; Some biochemical characteristics of Vibrio fetus and other related vibrios isolated from animals.. Journal of Bacteriology 76:312–316
    [Google Scholar]
  10. Loesche W. J., Gibbons R. J., Socransky S. S. 1965; Biochemical characteristics of Vibrio sputorum and relationship to Vibrio bubulus and Vibrio fetus. . Journal of Bacteriology 89:1109–1116
    [Google Scholar]
  11. Mccord J. M., Fridovich I. 1969; Superoxide dismutase. An enzymic function for erythrocup- rein (hemocuprein).. Journal of Biological Chemistry 244:6049–6055
    [Google Scholar]
  12. Niekus H. G. D., De Vries W., Stouthamer A. H. 1977; The effect of different dissolved oxygen tensions on growth and enzyme activities of Campylobacter sputorum subspecies bubulus. . Journal of General Microbiology 103:215–222
    [Google Scholar]
  13. Niekus H. G. D., Wouters C. H., De Vries W., Stouthamer A. H. 1978; Superoxide dismutase and hydrogen peroxide formation in Campylobacter sputorum subspecies bubulus. . Archives of Microbiology 119:37–42
    [Google Scholar]
  14. Sebald M., Véron M. 1963; Teneur en bases de l’ADN et classification des vibrions.. Annales de l’Institut Pasteur 105:897–910
    [Google Scholar]
  15. Smibert R. M. 1978; The genus Campylobacter. . Annual Review of Microbiology 32:673–709
    [Google Scholar]
  16. Stouthamer A. H., De Vries W., Niekus H. G. D. 1979; Microaerophily.. Antonie van Leeuwenhoek 45:5–12
    [Google Scholar]
  17. De Vries W., Niekus H. G. D., Boellaard M., Stouthamer A. H. 1980; Growth yields and energy generation by Campylobacter sputorum subspecies bubulus during growth in continuous culture with different hydrogen acceptors.. Archives of Microbiology 124:221–227
    [Google Scholar]
  18. Yonetani T., Ray G. S. 1965; Studies on cytochrome oxidase. VI. Kinetics of the aerobic oxidation of ferrocytochrome c by cytochrome oxidase.. Journal of Biological Chemistry 240:3392–3398
    [Google Scholar]
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