Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1978 Feb;133(2):477–484. doi: 10.1128/jb.133.2.477-484.1978

Sequence of b cytochromes relative to ubiquinone in the electron transport chain of Escherichia coli.

J A Downie, G B Cox
PMCID: PMC222048  PMID: 203570

Abstract

A ubiquinone-deficient mutant, carrying mutations in two genes affecting ubiquinone biosynthesis, has been used, in comparison with a normal strain, to determine the sequence of some of the components of the electron transport chain of Escherichia coli. The amounts of cytochromes reduced during aerobic steady-state conditions were estimated by comparing low-temperature difference spectra of normal or ubiquinone-deficient membranes with either D-lactate or reduced nicotinamide adenine dinucleotide as substrate. From the amounts of cytochromes reduced it was concluded that ubiquinone functions at two sites, one site being between the dehydrogenases and cytochromes and the second site being after cytochromes b562 and b556 but before cytochromes b558, d, and o. The scheme proposed is discussed in relation to the Mitchell protonmotive ubiquinone cycle.

Full text

PDF
477

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ashcroft J. R., Haddock B. A. Synthesis of alternative membrane-bound redox carriers during aerobic growth of Escherichia coli in the presence of potassium cyanide. Biochem J. 1975 May;148(2):349–352. doi: 10.1042/bj1480349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bachmann B. J., Low K. B., Taylor A. L. Recalibrated linkage map of Escherichia coli K-12. Bacteriol Rev. 1976 Mar;40(1):116–167. doi: 10.1128/br.40.1.116-167.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. CASTOR L. N., CHANCE B. Photochemical determinations of the oxidases of bacteria. J Biol Chem. 1959 Jun;234(6):1587–1592. [PubMed] [Google Scholar]
  4. CHANCE B., WILLIAMS G. R. The respiratory chain and oxidative phosphorylation. Adv Enzymol Relat Subj Biochem. 1956;17:65–134. doi: 10.1002/9780470122624.ch2. [DOI] [PubMed] [Google Scholar]
  5. Cox G. B., Gibson F., McCann L. M., Butlin J. D., Crane F. L. Reconstitution of the energy-linked transhydrogenase activity in membranes from a mutant strain of Escherichia coli K12 lacking magnesium ion- or calcium ion-stimulated adenosine triphosphatase. Biochem J. 1973 Apr;132(4):689–695. doi: 10.1042/bj1320689. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cox G. B., Gibson F., Pittard J. Mutant strains of Escherichia coli K-12 unable to form ubiquinone. J Bacteriol. 1968 May;95(5):1591–1598. doi: 10.1128/jb.95.5.1591-1598.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cox G. B., Newton N. A., Gibson F., Snoswell A. M., Hamilton J. A. The function of ubiquinone in Escherichia coli. Biochem J. 1970 Apr;117(3):551–562. doi: 10.1042/bj1170551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Garland P. B., Littleford S. J., Haddock B. A. A stopped-flow dual-wavelength spectrophotometer suitable for the study of respiratory chains. Biochem J. 1976 Feb 15;154(2):277–284. doi: 10.1042/bj1540277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gibson F., Cox G. B., Downie J. A., Radik J. A mutation affecting a second component of the F0 portion of the magnesium ion-stimulated adenosine triphosphatase of Escherichia coli K12. The uncC424 allele. Biochem J. 1977 Apr 15;164(1):193–198. doi: 10.1042/bj1640193. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Haddock B. A., Downie J. A., Garland P. B. Kinetic characterization of the membrane-bound cytochromes of Escherichia coli grown under a variety of conditions by using a stopped-flow dual-wavelength spectrophotometer. Biochem J. 1976 Feb 15;154(2):285–294. doi: 10.1042/bj1540285. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Haddock B. A., Schairer H. U. Electron-transport chains of Escherichia coli. Reconstitution of respiration in a 5-aminolaevulinic acid-requiring mutant. Eur J Biochem. 1973 May;35(1):34–45. doi: 10.1111/j.1432-1033.1973.tb02806.x. [DOI] [PubMed] [Google Scholar]
  12. Hendler R. W., Towne D. W., Shrager R. I. Redox properties of beta-type cytochromes in Escherichia coli and rat liver mitochondria and techniques for their analysis. Biochim Biophys Acta. 1975 Jan 31;376(1):42–62. doi: 10.1016/0005-2728(75)90203-0. [DOI] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. Mitchell P. Protonmotive redox mechanism of the cytochrome b-c1 complex in the respiratory chain: protonmotive ubiquinone cycle. FEBS Lett. 1975 Aug 1;56(1):1–6. doi: 10.1016/0014-5793(75)80098-6. [DOI] [PubMed] [Google Scholar]
  15. Mitchell P. The protonmotive Q cycle: a general formulation. FEBS Lett. 1975 Nov 15;59(2):137–139. doi: 10.1016/0014-5793(75)80359-0. [DOI] [PubMed] [Google Scholar]
  16. PITTARD J. EFFECT OF INTEGRATED SEX FACTOR ON TRANSDUCTION OF CHROMOSOMAL GENES IN ESCHERICHIA COLI. J Bacteriol. 1965 Mar;89:680–686. doi: 10.1128/jb.89.3.680-686.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Shipp W. S. Cytochromes of Escherichia coli. Arch Biochem Biophys. 1972 Jun;150(2):459–472. doi: 10.1016/0003-9861(72)90063-x. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES