1887

Abstract

The electron transport chain of grown anaerobically on glycerol with fumarate as terminal electron acceptor, has been studied using electron paramagnetic resonance (EPR) spectroscopy. The analysis did not include cytochromes, but was confined to the lower potential (dehydrogenase) section of the electron transport chain. Several ferredoxin-type centres were detected and partially characterized, and the possible presence of iron-sulphur centres paramagnetic in their oxidized form (‘HiPIP-type’) was also noted. An EPR-detectable signal that may have been due to the presence of molybdenum in the electron transport chain is described and assessed. Most of the centres detected were reducible by substrate in the absence of oxidant and some were found to be wholly or partly reduced during steady state oxidation of substrates in the presence of oxygen.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-129-6-1651
1983-06-01
2021-05-17
Loading full text...

Full text loading...

/deliver/fulltext/micro/129/6/mic-129-6-1651.html?itemId=/content/journal/micro/10.1099/00221287-129-6-1651&mimeType=html&fmt=ahah

References

  1. Barber M. J., Bray R. C., Cammack R., Coughlan M. P. 1977; Oxidation-reduction potentials of turkey liver xanthine dehydrogenase and the origins of oxidase and dehydrogenase behaviour in molybdenum containing hydroxylases. Biochemical Journal 163:279–289
    [Google Scholar]
  2. Blum H., Poole R. K., Ohnishi T. 1980; The orientation of iron-sulphur clusters in membrane multilayers prepared from aerobically-grown Escherichia coliK12 and a cytochrome deficient mutant. Biochemical Journal 190:385–393
    [Google Scholar]
  3. Boxer D. H., Malcolm A., Graham A. 1982; Escherichia coliformate to nitrate respiratory pathway: structural analysis. Biochemical Society Transactions 10:480–481
    [Google Scholar]
  4. Bray R. C. 1975; Molybdenum iron sulphurflavin hydroxylases and related enzymes. In The Enzymes 12 pp. 299–419 P. D. Boyer P. D. Edited by New York:: Academic Press.;
    [Google Scholar]
  5. Cohen G. N., Rickenberg H. W. 1956; Concentration specifique reversible des amino acides chez Escherichia coli. Annales de l’Institut Pasteur 91:693–720
    [Google Scholar]
  6. Cole S. T., Guest J. R. 1982; Molecular genetic aspects of the succinate: fumarateoxido-reductases of Escherichia coli. Biochemical Society Transactions 10:473–475
    [Google Scholar]
  7. Dutton P. L. 1978; Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron transfer systems. Methods in Enzymology 54:411–435
    [Google Scholar]
  8. Haddock B. A., Mandrand-Berthelot M-A. 1982; Escherichia coliformate to nitrate respiratory chain: genetic analysis. Biochemical Society Transactions 10:478–480
    [Google Scholar]
  9. Hamilton J. A., Cox G. B., Looney F. D., Gibson F. 1970; Ubisemiquinone in membranes from Escherichia coli. Biochemical Journal 116:319–320
    [Google Scholar]
  10. Hendler R. W., Burgess A. H. 1974; Fractionation of the electron-transport chain of Escherichia coli. Biochimica et biophysica acta 357:215–230
    [Google Scholar]
  11. Hendler R. W., Towne D. W., Shrager R. I. 1975; Redox properties of b-type cytochromes in Escherichia coliand rat liver mitochondria and techniques for their analysis. Biochimica et biophysica acta 376:42–62
    [Google Scholar]
  12. Ingledew W. J., Prince R. C. 1977; Thermodynamic resolution of the iron-sulphur centers of the succinic dehydrogenase of Rhodopseudomonas sphaeroides. Archives of Biochemistry and Biophysics 178:303–307
    [Google Scholar]
  13. Ingledew W. J., Reid G. A., Poole R. K., Blum H., Ohnishi T. 1980; The iron-sulphurcentres of aerobically grown Escherichia coliK12.An electron paramagnetic resonance study. FEBS Letters 111:223–227
    [Google Scholar]
  14. Kistler W. S., Lin E. C. C. 1972; Purification and properties of the flavine stimulated aerobic L-α-Glycerophosphate dehydrogenase of Escherichia coli. Journal of Bacteriology 112:539–547
    [Google Scholar]
  15. Nicholas D. J. D., Wilson P. W., Heinen W., Palmer G., Beinert H. 1962; Use of electron paramagnetic resonance spectroscopy in investigations of functional metal components in microorganisms. Nature; London: 196433–436
    [Google Scholar]
  16. Ohnishi T., Shirashi S., Ingledew W. J. 1976a; Resolution and functional characterization of two mitochondrial iron-sulphurcentres of the high potential iron-sulphur protein type. Biochemical Journal 153:39–48
    [Google Scholar]
  17. Ohnishi T., Salerno J. C., Winter D. B., Lim J., Yu C. A., Yu L., King T. E. 1976b; Thermodynamic and epr characteristics of two ferredoxin- type iron-sulphur centers in the succinate-ubiquinone reductase segment of the respiratory chain. Journal of Biological Chemistry 251:2094–2104
    [Google Scholar]
  18. Poole R. K., Haddock B. A. 1975; Effects of sulphate-limited growth in continuous culture on the electron transport chain and energy conservation in Escherichia coliK12. Biochemical Journal 152:537–546
    [Google Scholar]
  19. Poole R. K., Scott R. I., Chance B. 1980; Low temperature spectral and kinetic properties of cytochromes of Escherichia coliK12 grown at lowered oxygen tension. Biochimica et biophysica acta 591:471–482
    [Google Scholar]
  20. Pudek M. R., Bragg P. D. 1976; Redox potentials of the cytochromes in the respiratory chain of aerobically grown E. coli. Archives of Biochemistry and Biophysics 174:546–552
    [Google Scholar]
  21. Reid G. A., Ingledew W. J. 1979; Characterisation and phenotypic control of the cytochrome content of Escherichia coli. Biochemical Journal 182:465–472
    [Google Scholar]
  22. Shipp W. S. 1972; Cytochromes of Escherichia coli. Archives of Biochemistry and Biophysics 150:459–472
    [Google Scholar]
  23. Yoch D. C., Carithers R. P. 1979; Bacterial iron-sulphurcentres. Microbiological Reviews 43:384–421
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-129-6-1651
Loading
/content/journal/micro/10.1099/00221287-129-6-1651
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error