Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1962 Aug;84(2):368–382. doi: 10.1042/bj0840368

Selective inhibition by 2-heptyl-4-hydroxyquinoline N-oxide of certain oxidation–reduction reactions

Margot Kogut 1, J W Lightbown 1
PMCID: PMC1243678  PMID: 14457796

Full text

PDF
370

Selected References

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

  1. AVRON M. The inhibition of photoreactions of chloroplasts by 2-alkyl-4-hydroxyquinoline N-oxides. Biochem J. 1961 Apr;78:735–739. doi: 10.1042/bj0780735. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ainsworth S., Rabinowitch E. Electron Transfer and Absorption Spectra of Complexes. Science. 1960 Jan 29;131(3396):303–303. doi: 10.1126/science.131.3396.303. [DOI] [PubMed] [Google Scholar]
  3. BRAY R. C., MALMSTROM B. G., VANNGARD T. The chemistry of xanthine oxidase. Electron-spin resonance of xanthine oxidase solutions. Biochem J. 1959 Sep;73:193–197. doi: 10.1042/bj0730193. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. COMMONER B., HEISE J. J., LIPPINCOTT B. B., NORBERG R. E., PASSONNEAU J. V., TOWNSEND J. Biological activity of free radicals. Science. 1957 Jul 12;126(3263):57–63. doi: 10.1126/science.126.3263.57. [DOI] [PubMed] [Google Scholar]
  5. CORNFORTH J. W., JAMES A. T. Structure of a naturally occurring antagonist of dihydrostreptomycin. Biochem J. 1956 May;63(1):124–130. doi: 10.1042/bj0630124. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Coulthard C. E., Michaelis R., Short W. F., Sykes G. Notatin: an anti-bacterial glucose-aerodehydrogenase from Penicillium notatum Westling and Penicillium resticulosum sp. nov. Biochem J. 1945;39(1):24–36. doi: 10.1042/bj0390024. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. DOLIN M. I. The Streptococcus faecalis oxidases for reduced diphosphopyridine nucleotide. III. Isolation and properties of a flavin peroxidase for reduced diphosphopyridine nucleotide. J Biol Chem. 1957 Mar;225(1):557–573. [PubMed] [Google Scholar]
  8. DOLIN M. I. The Streptococus faecalis oxidases for reduced diphosphopyridine nucleotide. IV. Properties of the enzyme-substrate complex formed between reduced diphosphopyridine nucleotide peroxidase and pyridine nucleotides. J Biol Chem. 1960 Feb;235:544–550. [PubMed] [Google Scholar]
  9. EHRENBERG A., LUDWIG G. D. Free radical formation in reaction between old yellow enzyme and reduced triphosphopyridine nucleotide. Science. 1958 May 16;127(3307):1177–1178. doi: 10.1126/science.127.3307.1177. [DOI] [PubMed] [Google Scholar]
  10. Frisell W. R., Mackenzie C. G. THE PHOTOCHEMICAL OXIDATION OF DPNH WITH RIBOFLAVIN PHOSPHATE. Proc Natl Acad Sci U S A. 1959 Nov;45(11):1568–1572. doi: 10.1073/pnas.45.11.1568. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Isenberg I., Szent-Györgyi A. FREE RADICAL FORMATION IN RIBOFLAVIN COMPLEXES. Proc Natl Acad Sci U S A. 1958 Sep 15;44(9):857–862. doi: 10.1073/pnas.44.9.857. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. JACKSON F. L., LIGHTBOWN J. W. Inhibition of dihydrocozymase-oxidase activity of heart-muscle preparations and of certain cell-free bacterial preparations by 2-heptyl-4-hydroxyquinoline N-oxide. Biochem J. 1958 May;69(1):63–67. doi: 10.1042/bj0690063. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. KOGUT M., PODOSKI E. P. Oxidative pathways in a fluorescent Pseudomonas. Biochem J. 1953 Dec;55(5):800–811. doi: 10.1042/bj0550800. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. LIGHTBOWN J. W. An antagonist of streptomycin and dihydrostreptomycin produced by Pseudomonas aeruginosa. J Gen Microbiol. 1954 Dec;11(3):477–492. doi: 10.1099/00221287-11-3-477. [DOI] [PubMed] [Google Scholar]
  15. LIGHTBOWN J. W., JACKSON F. L. Inhibition of cytochrome systems of heart muscle and certain bacteria by the antagonists of dihydrostreptomycin: 2-alkyl-4-hydroxyquinoline N-oxides. Biochem J. 1956 May;63(1):130–137. doi: 10.1042/bj0630130. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. MARGOLIASH E. The chromatographic behaviour of cytochrome c on cation exchangers. Biochem J. 1954 Apr;56(4):535–543. doi: 10.1042/bj0560535. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. MARGOLIASH E. The use of ion exchangers in the preparation and purification of cytochrome c. Biochem J. 1954 Apr;56(4):529–535. doi: 10.1042/bj0560529. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. PULLMAN M. E., COLOWICK S. P., KAPLAN N. O. Comparison of diphosphopyridine nucleotide with its deaminated derivative in various enzyme systems. J Biol Chem. 1952 Feb;194(2):593–602. [PubMed] [Google Scholar]
  19. SMITH L., BALTSCHEFFSKY M. Respiration and light-induced phosphorylation in extracts of Rhodospirillum rubrum. J Biol Chem. 1959 Jun;234(6):1575–1579. [PubMed] [Google Scholar]
  20. TANIGUCHI S., ITAGAKI E. Nitrate reductase of nitrate respiration type from E. coli. I. Solubilization and purification from the particulate system with molecular characterization as a metalloprotein. Biochim Biophys Acta. 1960 Nov 4;44:263–279. doi: 10.1016/0006-3002(60)91562-6. [DOI] [PubMed] [Google Scholar]
  21. VERNON L. P., ASH O. K. The photo-reduction of pyridine nucleotides by illuminated chromatophores of Rhodospirillum rubrum in the presence of succinate. J Biol Chem. 1959 Jul;234(7):1878–1882. [PubMed] [Google Scholar]
  22. VERNON L. P. Photo-oxidations catalyzed by chromatophores of Rhodospirillum rubrum under anaerobic conditions. J Biol Chem. 1959 Jul;234(7):1883–1888. [PubMed] [Google Scholar]
  23. WHITBY L. G. A new method for preparing flavin-adenine dinucleotide. Biochem J. 1953 Jun;54(3):437–442. doi: 10.1042/bj0540437. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES