Abstract
Ferricytochrome c showed low-level chemiluminescence, with a light-emission measured of about 1×103–3×103 counts/s, when supplemented with organic hydroperoxides. Tertiary hydroperoxides (cumene hydroperoxide and t-butyl hydroperoxide) showed a saturation behaviour at about 5mm-hydroperoxide, whereas primary hydroperoxides showed a quadratic dependence on the hydroperoxide concentration. Chemiluminescence depended linearly on cytochrome c concentration, and optimal light-emission was observed at [t-butyl hydroperoxide]/[ferricytochrome c] ratios of 160–500. Hydroperoxide-supplemented ferricytochrome c consumed O2 at a rate of 1.0μmol/min per μmol of cytochrome c; the rate of O2 uptake was linearly related to the concentration of cytochrome c. The Soret absorption band of ferricytochrome c decreased about 64% after incubation with t-butyl hydroperoxide, whereas the 530nm band was almost totally abolished. Light-emission was (a) inhibited competitively by cyanide. (b) inhibited by singlet-oxygen quenchers (e.g. β-carotene), scavengers (e.g. dimethylfuran) and traps (e.g. histidine and tryptophan) and (c) increased by singlet-oxygen-chemiluminescence enhancer 1,4-diazabicyclo[2.2.2]-octane. Superoxide dismutase had no effect on the present system. The participation of free radicals is suggested by the effect of the radical trap 2,5-di-t-butylquinol. Singlet-oxygen dimol emission seems to be mainly responsible for the observed light-emission; a mechanism that can account for the major part of the present experimental observations is proposed.
Full text
PDF









Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Auclair C., Lecomte M. C. Singlet oxygen production associated with hydroperoxide induced lipid peroxidation in liver microsomes. Biochem Biophys Res Commun. 1978 Dec 14;85(3):946–951. doi: 10.1016/0006-291x(78)90635-6. [DOI] [PubMed] [Google Scholar]
- BANKS A., EDDIE E., SMITH J. G. Reactions of cytochrome-c with methyl linoleate hydroperoxide. Nature. 1961 Jun 3;190:908–909. doi: 10.1038/190908a0. [DOI] [PubMed] [Google Scholar]
- BUTT W. D., KEILIN D. Absorption spectra and some other properties of cytochrome c and of its compounds with ligands. Proc R Soc Lond B Biol Sci. 1962 Nov 20;156:429–458. doi: 10.1098/rspb.1962.0049. [DOI] [PubMed] [Google Scholar]
- Cadenas E., Boveris A., Chance B. Low-level chemiluminescence of bovine heart submitochondrial particles. Biochem J. 1980 Mar 15;186(3):659–667. doi: 10.1042/bj1860659. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chance B., Sies H., Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev. 1979 Jul;59(3):527–605. doi: 10.1152/physrev.1979.59.3.527. [DOI] [PubMed] [Google Scholar]
- DESAI I. D., TAPPEL A. L. DAMAGE TO PROTEINS BY PEROXIDIZED LIPIDS. J Lipid Res. 1963 Apr;4:204–207. [PubMed] [Google Scholar]
- Fridovich I. Superoxide dismutases. Annu Rev Biochem. 1975;44:147–159. doi: 10.1146/annurev.bi.44.070175.001051. [DOI] [PubMed] [Google Scholar]
- GEORGE P., TSOU C. L. Reaction between hydrocyanic acid, cyanide ion and ferricytochrome c. Biochem J. 1952 Feb;50(4):440–448. doi: 10.1042/bj0500440. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Halliwell B. Superoxide-dependent formation of hydroxyl radicals in the presence of iron chelates: is it a mechanism for hydroxyl radical production in biochemical systems? FEBS Lett. 1978 Aug 15;92(2):321–326. doi: 10.1016/0014-5793(78)80779-0. [DOI] [PubMed] [Google Scholar]
- Hawco F. J., O'Brien P. J. Singlet oxygen formation during hemoprotein catalyzed lipid peroxide decomposition. Biochem Biophys Res Commun. 1976 May 23;76(2):354–361. doi: 10.1016/0006-291x(77)90732-x. [DOI] [PubMed] [Google Scholar]
- Kaschnitz R. M., Hatefi Y. Lipid oxidation in biological membranes. Electron transfer proteins as initiators of lipid autoxidation. Arch Biochem Biophys. 1975 Nov;171(1):292–304. doi: 10.1016/0003-9861(75)90036-3. [DOI] [PubMed] [Google Scholar]
- 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]
- Matheson I. B., Etheridge R. D., Kratowich N. R., Lee J. The quenching of singlet oxygen by amino acids and proteins. Photochem Photobiol. 1975 Mar;21(3):165–171. doi: 10.1111/j.1751-1097.1975.tb06647.x. [DOI] [PubMed] [Google Scholar]
- McCord J. M., Day E. D., Jr Superoxide-dependent production of hydroxyl radical catalyzed by iron-EDTA complex. FEBS Lett. 1978 Feb 1;86(1):139–142. doi: 10.1016/0014-5793(78)80116-1. [DOI] [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]
- Misra H. P., Fridovich I. A peroxide-dependent reduction of cytochrome c by NADH. Biochim Biophys Acta. 1973 Apr 5;292(3):815–824. doi: 10.1016/0005-2728(73)90028-5. [DOI] [PubMed] [Google Scholar]
- Nakano M., Noguchi T., Sugioka K., Fukuyama H., Sato M. Spectroscopic evidence for the generation of singlet oxygen in the reduced nicotinamide adenine dinucleotide phosphate-dependent microsomal lipid peroxidation system. J Biol Chem. 1975 Mar 25;250(6):2404–2406. [PubMed] [Google Scholar]
- Nilsson R., Merkel P. B., Kearns D. R. Unambiguous evidence for the participation of singlet oxygen ( 1 ) in photodynamic oxidation of amino acids. Photochem Photobiol. 1972 Aug;16(2):117–124. doi: 10.1111/j.1751-1097.1972.tb07343.x. [DOI] [PubMed] [Google Scholar]
- Pryor W. A. The formation of free radicals and the consequences of their reactions in vivo. Photochem Photobiol. 1978 Oct-Nov;28(4-5):787–801. doi: 10.1111/j.1751-1097.1978.tb07020.x. [DOI] [PubMed] [Google Scholar]
- Roubal W. T., Tappel A. L. Damage to proteins, enzymes, and amino acids by peroxidizing lipids. Arch Biochem Biophys. 1966 Jan;113(1):5–8. doi: 10.1016/0003-9861(66)90150-0. [DOI] [PubMed] [Google Scholar]
- Sugioka K., Nakano M. A possible mechanism of the generation of singlet molecular oxygen in nadph-dependent microsomal lipid peroxidation. Biochim Biophys Acta. 1976 Feb 16;423(2):203–216. doi: 10.1016/0005-2728(76)90179-1. [DOI] [PubMed] [Google Scholar]
- TAPPEL A. L. The mechanism of the oxidation of unsaturated fatty acids catalyzed by hematin compounds. Arch Biochem Biophys. 1953 Jun;44(2):378–395. doi: 10.1016/0003-9861(53)90056-3. [DOI] [PubMed] [Google Scholar]
- TSOU C. L. Exogenous and endogenous cytochrome c. Biochem J. 1952 Feb;50(4):493–499. doi: 10.1042/bj0500493. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tomoda A., Sugimoto K., Suhara M., Takeshita M., Yoneyama Y. Haemichrome formation from haemoglobin subunits by hydrogen peroxide. Biochem J. 1978 May 1;171(2):329–335. doi: 10.1042/bj1710329. [DOI] [PMC free article] [PubMed] [Google Scholar]
