Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1990 Nov 1;271(3):707–712. doi: 10.1042/bj2710707

The cellular location and specificity of bacterial cytochrome c peroxidases.

C F Goodhew 1, I B Wilson 1, D J Hunter 1, G W Pettigrew 1
PMCID: PMC1149620  PMID: 2173903

Abstract

The locations of cytochrome c peroxidase and catalase activities in the two Gram-negative bacteria Pseudomonas stutzeri (N.C.I.B. 9721) and Paracoccus denitrificans (N.C.I.B. 8944) were investigated by the production of spheroplasts. In both species the cytochrome c peroxidase was predominantly periplasmic: 92% of total activity in Ps. stutzeri and 98% of nonmembrane-bound activity in Pa. denitrificans were found in this cellular compartment. In contrast, the catalase was mostly in the cytoplasmic fraction. Purification of the Pa. denitrificans cytochrome c peroxidase showed it to be the haem c-containing polypeptide of Mr 42,000 that has already been described by Bosma, Braster, Stouthamer & Van Versefeld [(1987) Eur. J. Biochem. 165, 665-670] but was not identified by them as a peroxidase. The visible-absorption spectra of the enzyme closely resemble those of cytochrome c peroxidase from Pseudomonas aeruginosa but the donor specificity is different, with the Pa. denitrificans enzyme preferring the basic mitochondrial cytochromes c to the acidic cytochromes c-551 and reacting well with the Pa. denitrificans cytochrome c-550.

Full text

PDF
707

Images in this article

709Fig. 2.
on p.709
710Fig. 3.
on p.710

Selected References

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

  1. Ambler R. P., Meyer T. E., Kamen M. D., Schichman S. A., Sawyer L. A reassessment of the structure of Paracoccus cytochrome c-550. J Mol Biol. 1981 Apr 5;147(2):351–356. doi: 10.1016/0022-2836(81)90445-9. [DOI] [PubMed] [Google Scholar]
  2. Ambler R. P., Wynn M. The amino acid sequences of cytochromes c-551 from three species of Pseudomonas. Biochem J. 1973 Mar;131(3):485–498. doi: 10.1042/bj1310485. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Berry E. A., Trumpower B. L. Isolation of ubiquinol oxidase from Paracoccus denitrificans and resolution into cytochrome bc1 and cytochrome c-aa3 complexes. J Biol Chem. 1985 Feb 25;260(4):2458–2467. [PubMed] [Google Scholar]
  4. Bosma G., Braster M., Stouthamer A. H., van Verseveld H. W. Subfractionation and characterization of soluble c-type cytochromes from Paracoccus denitrificans cultured under various limiting conditions in the chemostat. Eur J Biochem. 1987 Jun 15;165(3):665–670. doi: 10.1111/j.1432-1033.1987.tb11492.x. [DOI] [PubMed] [Google Scholar]
  5. Ellfolk N., Rönnberg M., Aasa R., Andréasson L. E., Vänngård T. Properties and function of the two hemes in Pseudomonas cytochrome c peroxidase. Biochim Biophys Acta. 1983 Feb 28;743(1):23–30. doi: 10.1016/0167-4838(83)90413-2. [DOI] [PubMed] [Google Scholar]
  6. Ellfolk N., Soininen R. Pseudomonas cytochrome c peroxidase. I. Purification procedure. Acta Chem Scand. 1970;24(6):2126–2136. doi: 10.3891/acta.chem.scand.24-2126. [DOI] [PubMed] [Google Scholar]
  7. Foote N., Thompson A. C., Barber D., Greenwood C. Pseudomonas cytochrome C-551 peroxidase. A purification procedure and study of CO-binding kinetics. Biochem J. 1983 Mar 1;209(3):701–707. doi: 10.1042/bj2090701. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Goodhew C. F., elKurdi A. B., Pettigrew G. W. The microaerophilic respiration of Campylobacter mucosalis. Biochim Biophys Acta. 1988 Mar 30;933(1):114–123. doi: 10.1016/0005-2728(88)90061-8. [DOI] [PubMed] [Google Scholar]
  9. Hunter D. J., Brown K. R., Pettigrew G. W. The role of cytochrome c4 in bacterial respiration. Cellular location and selective removal from membranes. Biochem J. 1989 Aug 15;262(1):233–240. doi: 10.1042/bj2620233. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Husain M., Davidson V. L. Characterization of two inducible periplasmic c-type cytochromes from Paracoccus denitrificans. J Biol Chem. 1986 Jul 5;261(19):8577–8580. [PubMed] [Google Scholar]
  11. Iwasaki H., Matsubara T. Cytochrome c-557 (551) and cytochrome cd of Alcaligenes faecalis. J Biochem. 1971 May;69(5):847–857. doi: 10.1093/oxfordjournals.jbchem.a129536. [DOI] [PubMed] [Google Scholar]
  12. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  13. Pettigrew G. W., Seilman S. Purification and properties of a cross-linked complex between cytochrome c and cytochrome c peroxidase. Biochem J. 1982 Jan 1;201(1):9–18. doi: 10.1042/bj2010009. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Rorth M., Jensen P. K. Determination of catalase activity by means of the Clark oxygen electrode. Biochim Biophys Acta. 1967 May 16;139(1):171–173. doi: 10.1016/0005-2744(67)90124-6. [DOI] [PubMed] [Google Scholar]
  15. Rönnberg M., Ellfolk N. Heme-linked properties of Pseudomonas cytochrome c peroxidase. Evidence for non-equivalence of the hemes. Biochim Biophys Acta. 1979 Dec 14;581(2):325–333. doi: 10.1016/0005-2795(79)90252-6. [DOI] [PubMed] [Google Scholar]
  16. Rönnberg M., Kalkkinen N., Ellfolk N. The primary structure of Pseudomonas cytochrome c peroxidase. FEBS Lett. 1989 Jul 3;250(2):175–178. doi: 10.1016/0014-5793(89)80714-8. [DOI] [PubMed] [Google Scholar]
  17. Rönnberg M., Osterlund K., Ellfolk N. Resonance Raman spectra of Pseudomonas cytochrome c peroxidase. Biochim Biophys Acta. 1980 Nov 20;626(1):23–30. doi: 10.1016/0005-2795(80)90193-2. [DOI] [PubMed] [Google Scholar]
  18. Scholes P. B., McLain G., Smith L. Purification and properties of a c-type cytochrome from Micrococcus denitrificans. Biochemistry. 1971 May 25;10(11):2072–2076. doi: 10.1021/bi00787a017. [DOI] [PubMed] [Google Scholar]
  19. Singh J., Wharton D. C. Cytochrome c-556, a di-heme protein from Pseudomonas aeruginosa. Biochim Biophys Acta. 1973 Feb 22;292(2):391–401. doi: 10.1016/0005-2728(73)90045-5. [DOI] [PubMed] [Google Scholar]
  20. Soininen R., Ellfolk N., Kalkkinen N. Pseudomonas cytochrome c peroxidase. IX. Molecular weight of the enzyme in dodecyl sulfate-polyacrylamide gel electrophoresis. Acta Chem Scand. 1973;27(3):1106–1107. doi: 10.3891/acta.chem.scand.27-1106. [DOI] [PubMed] [Google Scholar]
  21. Takio K., Titani K., Ericsson L. H., Yonetani T. Primary structure of yeast cytochrome c peroxidase. II. The complete amino acid sequence. Arch Biochem Biophys. 1980 Sep;203(2):615–629. doi: 10.1016/0003-9861(80)90219-2. [DOI] [PubMed] [Google Scholar]
  22. Thomas P. E., Ryan D., Levin W. An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Anal Biochem. 1976 Sep;75(1):168–176. doi: 10.1016/0003-2697(76)90067-1. [DOI] [PubMed] [Google Scholar]
  23. Villalaín J., Moura I., Liu M. C., Payne W. J., LeGall J., Xavier A. V., Moura J. J. NMR and electron-paramagnetic-resonance studies of a dihaem cytochrome from Pseudomonas stutzeri (ATCC 11607) (cytochrome c peroxidase). Eur J Biochem. 1984 Jun 1;141(2):305–312. doi: 10.1111/j.1432-1033.1984.tb08192.x. [DOI] [PubMed] [Google Scholar]
  24. Wood P. M. Periplasmic location of the terminal reductase in nitrite respiration. FEBS Lett. 1978 Aug 15;92(2):214–218. doi: 10.1016/0014-5793(78)80757-1. [DOI] [PubMed] [Google Scholar]
  25. Wood P. M. Why do c-type cytochromes exist? FEBS Lett. 1983 Dec 12;164(2):223–226. doi: 10.1016/0014-5793(83)80289-0. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES