1887

Abstract

Centrifugation of membrane vesicles, prepared from ultrasonically disrupted K12, on to a planar surface followed by slow, partial dehydration results in a high degree of parallel orientation of the membrane planes with respect to each other and the supporting surface. Rotation of such membrane multilayers about a single axis parallel with the membrane planes within the magnetic field of an electron paramagnetic resonance (e.p.r.) spectrometer allows the orientation of anisotropic paramagnetic centres to be deduced. Computer simulations of the angular dependence of cytochrome e.p.r. spectra show two, or perhaps three, cytochromes, well-oriented with respect to the membrane plane. A low-spin cytochrome is oriented with the normal to its haem plane lying in the membrane plane. One (or perhaps two) high-spin cytochrome(s) lies with its haem plane making an angle of 45° with the membrane plane. The orientation of the low-spin cytochrome haem is thus the same as that of haems in -type cytochromes and cytochrome oxidases of the type found in the mitochondria of higher animal and microbial cells and the bacterium ( Erecińska ., 1979 ). The possible identity of this low-spin component as the terminal oxidase, cytochrome , is discussed.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-119-1-145
1980-07-01
2021-05-14
Loading full text...

Full text loading...

/deliver/fulltext/micro/119/1/mic-119-1-145.html?itemId=/content/journal/micro/10.1099/00221287-119-1-145&mimeType=html&fmt=ahah

References

  1. Altendorf K. H., Staehelin L. A. 1974; Orientation of membrane vesicles from Escherichia coli as detected by freeze-cleave electron microscopy.. Journal of Bacteriology 117:888–899
    [Google Scholar]
  2. Blasie J. K., EreciŃska M., Samuels S., Leigh J. S. 1978; The structure of a cytochrome oxidase-lipid model membrane.. Biochimica et biophysica acta 501:33–52
    [Google Scholar]
  3. Blum H., Harmon H. J., Leigh J. S., Salerno J. C., Chance B. 1978a; The orientation of a heme of cytochrome c oxidase in submitochondrial particles.. Biochimica et biophysica acta 502:1–10
    [Google Scholar]
  4. Blum H., Salerno J. C., Leigh J. S. 1978b; A model for the simulation of the E.P.R. spectra of chromophores in partially oriented membrane multilayers.. Journal of Magnetic Resonance 30:385–391
    [Google Scholar]
  5. Blum H., Chance B., Litchfield W. J. 1978C; Effect of pH on bovine liver catalase as determined by electron paramagnetic resonance.. Biochimica et biophysica acta 534:317–321
    [Google Scholar]
  6. Blum H., Chance B., Gunson D. E., Litchfield W. J. 1978d; Electron paramagnetic resonance spectra of myeloperoxidase in polymorphonuclear leukocytes.. FEES Letters 86:37–41
    [Google Scholar]
  7. Blumberg W. E. 1967; The EPR of high spin Fe3+ in rhombic fields. . In Magnetic Resonance in Biological Systems pp. 119–133 Ehrenberg A., Malström B. G., Vänngard T. Edited by Oxford: Pergamon Press;
    [Google Scholar]
  8. Castor L. N., Chance B. 1959; Photochemical determinations of the oxidases of bacteria.. Journal of Biological Chemistry 234:1587–1592
    [Google Scholar]
  9. Crane F. L., Glenn J. L., Green D. E. 1956; Studies on the electron transfer system. IV. The electron transfer particle.. Biochimica et biophysica acta 22:475–487
    [Google Scholar]
  10. Downie J. A., Cox G. B. 1978; Sequence of b cytochromes relative to ubiquinone in the electron transport chain of Escherichia coli. . Journal of Bacteriology 133:477–484
    [Google Scholar]
  11. Erecińska M., Blasie J. K., Wilson D. F. 1977; . Orientation of the hemes of cytochrome c oxidase and cytochrome c in mitochondria.. FEBS Letters 76:235–239
    [Google Scholar]
  12. Erecińska M., Wilson D. F., Blasie J. K. 1978; . Studies on the orientations of the mitochondrial redox carriers. II. Orientation of the mitochondrial chromophores with respect to the plane of the membrane in hydrated, oriented mitochondrial multilayers.. Biochimica et biophysica acta 501:63–71
    [Google Scholar]
  13. Erecińska M., Wilson D. F., Blasie J. K. 1979; . Studies of the orientation of the mitochondrial redox carriers. III. Orientation of the gK and gy axes of the hemes of cytochrome oxidase with respect to the plane of the membrane in oriented membrane multilayers.. Biochimica et biophysica acta 545:352–364
    [Google Scholar]
  14. Garland P. B. 1979; Vectorial oxidoreductions of bacterial respiratory chains.. Xlth International Congress of Biochemistry Toronto, Canada: 1979 Abstract 06-7-Smp 4
    [Google Scholar]
  15. Garland P. B., Davison M. T., Moore C. H. 1979; Rotational mobility of membrane-bound cytochrome o of Escherichia coli and cytochrome a1 of Thiobacillus ferro-oxidans.. Biochemical Society Transactions 7:1112–1114
    [Google Scholar]
  16. Haddock B. A., Jones C. W. 1977; Bacterial respiration.. Bacteriological Reviews 41:47–99
    [Google Scholar]
  17. Haddock B. A., Downie J. A., Garland P. B. 1976; Kinetic characterization of the membrane- bound cytochromes of Escherichia coli grown under a variety of conditions by using a stopped- flow dual-wavelength spectrophotometer.. Biochemical Journal 154:285–294
    [Google Scholar]
  18. Hendler R. W., Towne D. W., Schrager R. I. 1975; Redox properties of b-type cytochromes in Escherichia coli and rat liver mitochondria and techniques for their analysis.. Biochimica et biophysica acta 376:42–62
    [Google Scholar]
  19. Junge W., Devault D. 1975; Symmetry, orientation and rotational mobility in the a3 haem of cytochrome c oxidase in the inner membrane of mitochondria.. Biochimica et biophysica acta 408:200–214
    [Google Scholar]
  20. Kaback H. R. 1971; Bacterial membranes.. Methods in Enzymology 22:99–120
    [Google Scholar]
  21. Knowles P. F., Marsh D., Rattle H. W. E. 1976 Magnetic Resonance of Biomolecules pp. 168–207 London: John Wiley;
    [Google Scholar]
  22. Peisach J., Blumberg W. E., Ogawa S., Rach-Milewitz E. A., Oltzik R. 1971; The effects of protein conformation on the heme symmetry in high spin ferric heme proteins as studied by electron paramagnetic resonance.. Journal of Biological Chemistry 246:3342–3355
    [Google Scholar]
  23. Poole R. K., Haddock B. A. 1974; Energy- linked reduction of nicotinamide-adenine dinucleotide in membranes derived from normal and various respiratory-deficient mutant strains of Escherichia coli K12.. Biochemical Journal 144:77–85
    [Google Scholar]
  24. 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 coli K12.. Biochemical Journal 152:537–546
    [Google Scholar]
  25. Poole R. K., Waring A. J., Chance B. 1979a; Evidence for a functional oxygen-bound intermediate in the reaction of Escherichia coli cytochrome o with oxygen.. FEBS Letters 101:56–58
    [Google Scholar]
  26. Poole R. K., Waring A. J., Chance B. 1979b; The reaction of cytochrome o in Escherichia coli with oxygen. Low temperature kinetic and spectral properties.. Biochemical Journal 184:379–389
    [Google Scholar]
  27. Pudek M. R., Bragg P. D. 1976; Redox potentials of the cytochromes in the respiratory chain of aerobically-grown Escherichia coli.. Archives of Biochemistry and Biophysics 174:546–552
    [Google Scholar]
  28. Reid G. A., Ingledew W. J. 1979; Characterization and phenotypic control of the cytochrome content of Escherichia coli. . Biochemical Journal 182:465–472
    [Google Scholar]
  29. Salerno J. C., Blum H., Ohnishi T. 1979; The orientation of iron-sulfur clusters and a spincoupled ubiquinone pair in the mitochondrial membrane.. Biochimica et biophysica acta 547:270–281
    [Google Scholar]
  30. Shipp W. S. 1972; Cytochromes of Escherichia coli.. Archives of Biochemistry and Biophysics 150:459–472
    [Google Scholar]
  31. Tiede D. M., Leigh J. S., Dutton P. L. 1978; Structural organization of the Chromatium vinosum reaction center associated c-cytochromes.. Biochimica et biophysica acta 503:524–544
    [Google Scholar]
  32. Van Gelder B. F., Orme-Johnson W. H., Hansen R. E., Beinert H. 1967; Electron paramagnetic resonance of haem at intermediate oxidation states of cytochrome c oxidase.. Proceedings of the National Academy of Sciences of the United States of America 58:1073–1079
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-119-1-145
Loading
/content/journal/micro/10.1099/00221287-119-1-145
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