Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1972 Nov;69(11):3432–3435. doi: 10.1073/pnas.69.11.3432

On the Monoheme Character of Cytochromes c

S J Kennel 1,*, T E Meyer 1, M D Kamen 1,, R G Bartsch 1
PMCID: PMC389787  PMID: 4343972

Abstract

Interpretations of data bearing on structures of cytochromes cc′—a class of variant c-type heme proteins from bacteria—in support of a diheme-bearing single chain as a basic structural unit, appear to be invalid in the light of recent studies. These reveal that nearly all members of this class exist as dimers that can be dissociated into, if they do not already exist as, monoheme-bearing monomers. The particular case of the Chromatium protein, held to be the source of a peptic-“core” peptide containing two covalently-bonded heme groups, has been re-examined by preparation of tryptic and chymotryptic peptides derived from the heme-bearing region of the protein, as well as by repetition of experiments on peptic digestion, with more rigorous purification of the resultant peptides than was previously done. It is shown that this protein can also be dissociated into identical subunits, bearing a single heme prosthetic group, and accounting essentially for all its heme content. Thus, the previous terminology—cytochromes cc′—based on supposition of heme group heterogeneity, is inconsistent with these findings and should be replaced by cytochromes c′.

Keywords: monoheme peptide, heme, subunit structure, cytochrome nomenclature

Full text

PDF
3432

Selected References

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

  1. Ambler R. P., Brown L. H. The amino acid sequence of Pseudomonas fluorescens azurin. Biochem J. 1967 Sep;104(3):784–825. doi: 10.1042/bj1040784. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ambler R. P., Bruschi M., Le Gall J. The structure of cytochrome c'(3) from desulfovibrio gigas (NCIB 9332). FEBS Lett. 1969 Oct 21;5(2):115–117. doi: 10.1016/0014-5793(69)80308-x. [DOI] [PubMed] [Google Scholar]
  3. BARRETT J., KAMEN M. D. On the prosthetic group of an RHP-type haem protein from Chromatium. Biochim Biophys Acta. 1961 Jul 8;50:573–575. doi: 10.1016/0006-3002(61)90019-1. [DOI] [PubMed] [Google Scholar]
  4. BARTSCH R. G., COVAL M. L., KAMEN M. D. The amino acid composition of the soluble chromatium haem proteins. Biochim Biophys Acta. 1961 Aug 5;51:241–245. doi: 10.1016/0006-3002(61)90164-0. [DOI] [PubMed] [Google Scholar]
  5. BARTSCH R. G., KAMEN M. D. Isolation and properties of two soluble heme proteins in extracts of the photoanaerobe Chromatium. J Biol Chem. 1960 Mar;235:825–831. [PubMed] [Google Scholar]
  6. BARTSCH R. G., KAMEN M. D. On the new heme protein of facultative photoheterotrophs. J Biol Chem. 1958 Jan;230(1):41–63. [PubMed] [Google Scholar]
  7. Bartsch R. G. Bacterial cytochromes. Annu Rev Microbiol. 1968;22:181–200. doi: 10.1146/annurev.mi.22.100168.001145. [DOI] [PubMed] [Google Scholar]
  8. Cusanovich M. A. Molecular weights of some cytochromes cc'. Biochim Biophys Acta. 1971 Apr 27;236(1):238–241. doi: 10.1016/0005-2795(71)90171-1. [DOI] [PubMed] [Google Scholar]
  9. Cusanovich M. A., Tedro S. M., Kamen M. D. Pseudomonas denitrificans cytochrome cc'. Arch Biochem Biophys. 1970 Dec;141(2):557–570. doi: 10.1016/0003-9861(70)90175-x. [DOI] [PubMed] [Google Scholar]
  10. DEKLERK H., BARTSCH R. G., KAMEN M. D. ATYPICAL SOLUBLE HAEM PROTEINS FROM A STRAIN OF RHODOPSEUDOMONAS PALUSTRIS SP. Biochim Biophys Acta. 1965 Feb 15;97:275–280. doi: 10.1016/0304-4165(65)90092-9. [DOI] [PubMed] [Google Scholar]
  11. DOOLITTLE R. F. CHARACTERIZATION OF LAMPREY FIBRINOPEPTIDES. Biochem J. 1965 Mar;94:742–750. doi: 10.1042/bj0940742. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. DUS K., KAMEN M. D. COMPARATIVE STRUCTURAL STUDIES ON SOME BACTERIAL HEME PROTEINS. Biochem Z. 1963;338:364–375. [PubMed] [Google Scholar]
  13. Dus K., de Klerk H., Bartsch R. G., Horio T., Kamen M. D. ON THE MONOHEME NATURE OF CYTOCHROME c' (Rhodopseudomonas palustris). Proc Natl Acad Sci U S A. 1967 Feb;57(2):367–370. doi: 10.1073/pnas.57.2.367. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. HIRS C. H. The oxidation of ribonuclease with performic acid. J Biol Chem. 1956 Apr;219(2):611–621. [PubMed] [Google Scholar]
  15. HORIO T., KAMEN M. D., DE KLERK H. Relative oxidation-reduction potentials of heme groups in two soluble doubleheme proteins. J Biol Chem. 1961 Oct;236:2783–2787. [PubMed] [Google Scholar]
  16. Kamen M. D., Horio T. Bacterial cytochromes. I. Structural aspects. Annu Rev Biochem. 1970;39:673–700. doi: 10.1146/annurev.bi.39.070170.003325. [DOI] [PubMed] [Google Scholar]
  17. Meyer T. E., Cusanovich M. A. Euglena gracilis cytochrome 558. Biochim Biophys Acta. 1972 May 25;267(2):383–387. doi: 10.1016/0005-2728(72)90125-9. [DOI] [PubMed] [Google Scholar]
  18. Pettigrew G. W. The amino acid sequence of a cytochrome c from a protozoan Crithidia oncopelti. FEBS Lett. 1972 Apr 15;22(1):64–66. doi: 10.1016/0014-5793(72)80220-5. [DOI] [PubMed] [Google Scholar]
  19. SJOQUIST J. Determination of amino acids as phenyl thiohydantoin derivatives. III. Quantitative determination of 3-phenyl-2-thiohydantoins from paper chromatograms. Biochim Biophys Acta. 1960 Jun 17;41:20–30. doi: 10.1016/0006-3002(60)90364-4. [DOI] [PubMed] [Google Scholar]
  20. SUZUKI H., IWASAKI H. Studies on denitrification. VI. Preparations and properties of crystalline blue protein and cryptocytochrome c, and role of copper in denitrifying enzyme from a denitrifying bacterium. J Biochem. 1962 Sep;52:193–199. doi: 10.1093/oxfordjournals.jbchem.a127596. [DOI] [PubMed] [Google Scholar]
  21. Stanier R. Y., Palleroni N. J., Doudoroff M. The aerobic pseudomonads: a taxonomic study. J Gen Microbiol. 1966 May;43(2):159–271. doi: 10.1099/00221287-43-2-159. [DOI] [PubMed] [Google Scholar]
  22. VERNON L. P., KAMEN M. D. Hematin compounds in photosynthetic bacteria. J Biol Chem. 1954 Dec;211(2):643–662. [PubMed] [Google Scholar]
  23. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES