Abstract
As a highly reactive substance produced in biological systems by the one-electron reduction of oxygen, superoxide (O2-) seemed a likely candidate as a bactericidal agent in leukocytes. The reduction of cytochrome c, a process in which O2- may serve as an electron donor, was found to occur when the cytochrome was incubated with leukocytes. O2- was identified as the agent responsible for the leukocyte-mediated reduction of cytochrome c by the demonstration that the reaction was abolished by superoxide dismutase, an enzyme that destroys O2-, but not by boiled dismutase, albumin, or catalase.
Leukocyte O2- production doubled in the presence of latex particles. The average rate of formation of O2- in the presence of these particles was 1.03 nmol/107 cells per 15 min. This rate, however, is only a lower limit of the true rate of O2- production, since any O2- which reacted with constituents other than cytochrome c would have gone undetected. Thus. O2- is made by leukocytes under circumstances which suggest that it may be involved in bacterial killing.
Full text
PDF![741](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48bf/302313/0ffe8dd07c8e/jcinvest00179-0213.png)
![742](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48bf/302313/02d19d277f06/jcinvest00179-0214.png)
![743](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48bf/302313/793382398255/jcinvest00179-0215.png)
![744](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48bf/302313/7e5a839490e5/jcinvest00179-0216.png)
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Hirata F., Hayaishi O. Possible participation of superoxide anion in the intestinal tryptophan 2,3-dioxygenase reaction. J Biol Chem. 1971 Dec 25;246(24):7825–7826. [PubMed] [Google Scholar]
- Karnovsky M. L. The metabolism of leukocytes. Semin Hematol. 1968 Apr;5(2):156–165. [PubMed] [Google Scholar]
- Klebanoff S. J. Iodination of bacteria: a bactericidal mechanism. J Exp Med. 1967 Dec 1;126(6):1063–1078. doi: 10.1084/jem.126.6.1063. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lehrer R. I., Cline M. J. Interaction of Candida albicans with human leukocytes and serum. J Bacteriol. 1969 Jun;98(3):996–1004. doi: 10.1128/jb.98.3.996-1004.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MARGOLIASH E., FROHWIRT N. Spectrum of horse-heart cytochrome c. Biochem J. 1959 Mar;71(3):570–572. doi: 10.1042/bj0710570. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McCord J. M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049–6055. [PubMed] [Google Scholar]
- Nathan D. G., Baehner R. L. Disorders of phagocytic cell function. Prog Hematol. 1971;7(0):235–254. [PubMed] [Google Scholar]
- Paul B., Sbarra A. J. The role of the phagocyte in host-parasite interactions. 13. The direct quantitative estimation of H2O2 in phagocytizing cells. Biochim Biophys Acta. 1968 Feb 1;156(1):168–178. doi: 10.1016/0304-4165(68)90116-5. [DOI] [PubMed] [Google Scholar]
- SBARRA A. J., KARNOVSKY M. L. The biochemical basis of phagocytosis. I. Metabolic changes during the ingestion of particles by polymorphonuclear leukocytes. J Biol Chem. 1959 Jun;234(6):1355–1362. [PubMed] [Google Scholar]
- Strobel H. W., Coon M. J. Effect of superoxide generation and dismutation on hydroxylation reactions catalyzed by liver microsomal cytochrome P-450. J Biol Chem. 1971 Dec 25;246(24):7826–7829. [PubMed] [Google Scholar]
- Woeber K. A., Doherty G. F., Ingbar S. H. Stimulation by phagocytosis of the deiodination of L-thyroxine in human leukocytes. Science. 1972 Jun 2;176(4038):1039–1041. doi: 10.1126/science.176.4038.1039. [DOI] [PubMed] [Google Scholar]
- YAMAZAKI I., PIETTE L. H. THE MECHANISM OF AEROBIC OXIDASE REACTION CATALYZED BY PEROXIDASE. Biochim Biophys Acta. 1963 Sep 3;77:47–64. doi: 10.1016/0006-3002(63)90468-2. [DOI] [PubMed] [Google Scholar]