Oxene Donors Yield Low‐Level Chemiluminescence with Microsomes and Isolated Cytochrome P‐450
Open accessAbstract
Microsomes supplemented with different oxene donors yield light emission. The ability of oxene donors to support monooxygenation paralleled the observed chemiluminescence intensities, and the following order was observed: iodosobenzene > cumene hydroperoxide >t‐butyl hydroperoxide > H 2 O 2. Pyridine‐N‐oxide, which was reported to be effective in the bacterial camphor monooxygenase, showed neither O‐dealkylation of ethoxycoumarin nor chemiluminescence activity. Iodosobenzene‐induced chemiluminescence was not associated with high malondialdehyde accumulation, at variance with t‐butyl hydroperoxide, the lower light emission intensity of which was largely accompanied by lipid peroxidation, predominantly in a second phase of chemiluminescence. The ratio of maximal malondial‐dehyde formed/maximal chemiluminescence intensity was 30‐fold higher for t‐butyl hydroperoxide than for iodosobenzene. Low‐level chemiluminescence elicited by iodosobenzene was identified spectrally to be due, at least in part, to singlet oxygen, because of similar photoemission intensities at 634 nm and 703 nm (singlet oxygen dimol emission) and low intensity at 668 nm. Reducing equivalents to cytochrome P‐450, NADPH or NADH, exerted an inhibitory effect on iodosobenzene‐induced chemiluminescence. Aminopyrine, a substrate for microsomal monooxyganases, inhibited chemiluminescence, probably by favoring hydroxylation. Oxene donor‐supplemented isolated cytochrome P‐450 yielded low‐level chemiluminescence and the order of efficiency of the oxene donors mirrored that observed with intact microsomes. The fact that microsomes and ferricytochrome P‐450 supplemented with oxene donors yield chemiluminescence (identified partly as singlet oxygen dimol emission) is discussed in terms of heterolytic versus homolytic cleavage of the O‐O bond of hydroperoxides.
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The Ullrich/Cadenas/Sies group found that heme enzymes cytochrome P450 and cyclooxygenase generate red luminescence attributable to O2 excited by energy transfer from triplet-state enzyme products.
“the Ullrich/Cadenas/Sies group found that the heme enzymes cytochrome P450 and cyclooxygenase generate red luminescence attributable to O2 excited by energy transfer from triplet-state enzyme products”
From Chemiexcitation: Mammalian Photochemistry in the Dark<sup>†</sup> (2023) · cites this paper as [25]
The section on iodosobenzene-induced chemiluminescence reports red-region emission from cytochrome P-450 systems and identifies part of it as singlet-oxygen dimol emission. The paper does not report cyclooxygenase producing that light or attribute the oxygen excitation to energy transfer from triplet-state enzyme products; its proposed mechanism instead involves an active oxygen complex reacting with an oxene donor. (LLM, conf=0.88)
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Self-citation
- Authors
- CADENAS, E., SIES, H., GRAF, H., & ULLRICH, V.
- Affiliations
- Heinrich Heine University Düsseldorf (DE)
- Saarland University (DE)
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1983-01
- Volume
- 130
- Issue
- 1
- Pages
- 117-121
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W2053011341
- Cited by
- 44
- References
- 22
- Citations by year
- 2023: 1
- FWCI
- 2.54
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- European Journal of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › bioluminescence and chemiluminescence research
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- chemiluminescence, cytochrome P450, microsomes, iodosobenzene, cumene hydroperoxide, tert-butyl hydroperoxide, hydrogen peroxide, singlet oxygen, lipid peroxidation, malondialdehyde, NADPH, NADH, aminopyrine
- MeSH terms
- Animals, Cytochrome P-450 Enzyme System, Iodobenzenes, Luminescent Measurements, Microsomes, Liver, Oxidation-Reduction, Oxygen, Peroxides, Spectrophotometry, tert-Butylhydroperoxide, Rats
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