Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1949;45(1):14–30. doi: 10.1042/bj0450014

A respiratory catalyst required for the reduction of cytochrome c by cytochrome b

E C Slater 1
PMCID: PMC1274934  PMID: 16748583

Full text

PDF
30

Selected References

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

  1. Bach S. J., Dixon M., Zerfas L. G. Yeast lactic dehydrogenase and cytochrome b(2). Biochem J. 1946;40(2):229–239. [PMC free article] [PubMed] [Google Scholar]
  2. Barron E. S., Miller Z. B., Kalnitsky G. The oxidation of dithiols. Biochem J. 1947;41(1):62–68. doi: 10.1042/bj0410062. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Barron E. S., Miller Z. B., Meyer J. The effect of 2:3-dimercaptopropanol on the activity of enzymes and on the metabolism of tissues. Biochem J. 1947;41(1):78–82. doi: 10.1042/bj0410078. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hopkins F. G., Morgan E. J., Lutwak-Mann C. The influence of thiol groups in the activity of dehydrogenases. II: With an addendum on the location of dehydrogenases in muscle. Biochem J. 1938 Oct;32(10):1829–1848. doi: 10.1042/bj0321829. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hopkins F. G., Morgan E. J. The influence of thiol-groups in the activity of dehydrogenases. Biochem J. 1938 Mar;32(3):611–620. doi: 10.1042/bj0320611. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Keilin D., Hartree E. F. Activity of the succinic dehydrogenase-cytochrome system in different tissue preparations. Biochem J. 1949;44(2):205–218. doi: 10.1042/bj0440205. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Keilin D., Hartree E. F. Properties of azide-catalase. Biochem J. 1945;39(2):148–157. doi: 10.1042/bj0390148. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Keilin D., Hartree E. F. Properties of catalase. Catalysis of coupled oxidation of alcohols. Biochem J. 1945;39(4):293–301. [PMC free article] [PubMed] [Google Scholar]
  9. Keilin D., Hartree E. F. Purification and properties of cytochrome c. Biochem J. 1945;39(4):289–292. doi: 10.1042/bj0390289. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Lemberg R., Legge J. W., Lockwood W. H. Coupled oxidation of ascorbic acid and haemoglobin: Formation and properties of choleglobin. Biochem J. 1941 Mar;35(3):328–338. doi: 10.1042/bj0350328. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. McFarlane W. D. Application of the sodium diethyldithiocarbamate reaction to the micro-colorimetric determination of copper in organic substances. Biochem J. 1932;26(4):1022–1033. doi: 10.1042/bj0261022. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Pirie N. W. The preparation of glutathione from yeast and liver. Biochem J. 1930;24(1):51–54. doi: 10.1042/bj0240051. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Proceedings of the Biochemical Society. Biochem J. 1948;42(1):i.1–i.x. [PMC free article] [PubMed] [Google Scholar]
  14. Quastel J. H., Wheatley A. H. The relation of thiol compounds to glucose fermentation. Biochem J. 1932;26(6):2169–2176. doi: 10.1042/bj0262169. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Slater E. C. A comparative study of the succinic dehydrogenase-cytochrome system in heart muscle and in kidney. Biochem J. 1949;45(1):1–8. doi: 10.1042/bj0450001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Slater E. C. The action of inhibitors on the system of enzymes which catalyse the aerobic oxidation of succinate. Biochem J. 1949;45(1):8–13. doi: 10.1042/bj0450008. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Slater E. C. The measurement of the cytochrome oxidase activity of enzyme preparations. Biochem J. 1949;44(3):305–318. doi: 10.1042/bj0440305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Webb E. C., Van Heyningen R. The action of British anti-lewisite (BAL) on enzyme systems. Biochem J. 1947;41(1):74–78. doi: 10.1042/bj0410074. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES