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PubMed1991

Mechanism for the generation of superoxide anion and singlet oxygen during heme compound-catalyzed linoleic acid hydroperoxide decomposition.

Heme compound, hematin or cytochrome c, catalyzes the decomposition of 13-hydroperoxy linoleic acid yielding both O2- and 1O2 under aerobic conditions. No 1O2 is produced when hydrogen peroxide and cumene hydroperoxide are used as substrates. In these experiments, both O2- and 1O2 could be precisely detected by a chemiluminescence method using a cypridina luciferin analog, 2-methyl-6-(p-methoxyphenyl)-3,7-dihydroimidazo[1,2-a]pyrazin++ +-3-one, as a chemiluminescence probe, in the absence and presence of Cu-Zn superoxide dismutase in catalytic amounts. The reduction and oxidation cycle of ferric heme compound and the bimolecular reaction of peroxyl radicals are plausible reaction mechanisms for O2- and 1O2 production, respectively, in the systems studied.

Catalysis↗
PubMed1991

The singlet oxygen and carotenoid interaction.

Second-order rate constants kQ for the quenching of O2(1 delta g) by carotenoids were determined at room temperature in benzene and toluene using the technique of time-resolved luminescence. Of the C40 pigments studied, lycopene was found to be the most efficient quencher, but the increased efficiency compared with all-trans beta-carotene was less than previously reported. The efficiency of quenching of O2(1 delta g) was extended to a number of solvents with varying viscosities. kQ was found to be inversely proportional to solvent viscosity, although the relationship is not simply linear. The results suggest the involvement of thermodynamic factors. The efficiency of deactivation of O2(1 delta g) was found to increase with the number of conjugated carbon-carbon double bonds, i.e. kQ(C60) greater than kQ(C50) greater than kQ(C40). A number of xanthophylls were included in this study; it would appear that an epoxide group rather than carbonyl or hydroxyl substituents increase the reactivity of the carotenoid with respect to O2(1 delta g).

Carotenoids↗
PubMed2004

Formation of radicals from singlet oxygen produced during photoinhibition of isolated light-harvesting proteins of photosystem II.

Electron spin resonance spectroscopy and liquid chromatography have been used to detect radical formation and fragmentation of polypeptides during photoinhibition of purified major antenna proteins, free of protease contaminants. In the absence of oxygen and light, no radicals were observed and there was no damage to the proteins. Similarly illumination of the apoproteins did not induce any polypeptide fragmentation, suggesting that chlorophyll, light and atmospheric oxygen are all participating in antenna degradation. The use of TEMP and DMPO as spin traps showed that protein damage initiates with generation of (1)O(2), presumably from a triplet chlorophyll, acting as a Type II photosensitizer which attacks directly the amino acids causing a complete degradation of protein into small fragments, without the contribution of proteases. Through the use of scavengers, it was shown that superoxide and H(2)O(2) were not involved initially in the reaction mechanism. A higher production of radicals was observed in trimers than in monomeric antenna, while radical production is strongly reduced when antennae were organized in the photosystem II (PSII) complex. Thus, monomerization of antennae as well as their incorporation into the PSII complex seem to represent physiologically protected forms. A comparison is made of the photoinhibition mechanisms of different photosynthetic systems.

Electron Spin Resonance Spectroscopy↗