Abstract
Summary Chlorophylls were degraded by soluble proteins extracted from leaves of Chenopodium album . The bleaching (oxidative cleavage) of chlorophylls and accumulation of pheophorbides were observed. The accumulation of pheophorbides was not inhibited by anoxygenic conditions or by ascorbate, but the bleaching of chlorophylls was inhibited. It appears that there are two distinct degradation pathways: chlorophyll bleaching and pheophorbide accumulation in the process of chlorophyll breakdown. The bleaching reaction was not affected by hydrogen peroxide or hydrogen peroxide and 2,6-dichloroindophenol, but was slightly inhibited by linolenic acid. Catalase had no effect, but superoxide dismutase inhibited weakly. This bleaching was strongly inhibited by tiron and ascorbate. These results suggest that active oxygen, probably the superoxide radical, may be involved, but the enzymes catalase, peroxidase, and lipoxidase are not responsible for the bleaching reaction. The accumulation of pheophorbide derivatives is discussed in relation to the inhibition of bleaching activity.
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