Format

Send to

Choose Destination
Arch Biochem Biophys. 1986 Dec;251(2):567-76.

Photoinactivation of catalase in vitro and in leaves.

Abstract

Purified catalase from bovine liver and catalase of isolated intact peroxisomes from rye leaves were inactivated in vitro by irradiation with visible light. During photoinactivation the protein moiety of pure catalase was not cleaved; however, the electrophoretic mobility of the native enzyme was decreased, and a major portion of enzyme-bound heme was dissociated. In a suspension of isolated chloroplasts photoinactivation of pure or peroxisomal catalase was mediated by light absorption in the chloroplasts. Both the direct and the chloroplast-mediated photoinactivation of catalase were affected little by the presence of D2O or superoxide dismutase but were greatly retarded by formate. In isolated peroxisomes substantial photoinactivation of catalase occurred only in the presence of nonphotosynthesizing but not in the presence of photosynthesizing isolated chloroplasts. Substantial and selective photoinactivation of catalase was also observed in vivo when leaf sections from various plant species (rye, pea, sunflower, cucumber, maize) were irradiated with light of high intensity in the presence of the translation inhibitors cycloheximide or 2-(4-methyl-2,6-dinitroanilino)-N-methylpropionamide, while catalase activity was much less or not affected in 3-(3,4-dichlorophenyl)-1,1-dimethylurea-treated or untreated control sections. The extent of photoinactivation of catalase in leaves depended on light intensity and also occurred in red light. The results suggest that photoinactivation of catalase generally occurs in leaves under high light intensity, though it is not apparent under normal physiological conditions because it is compensated for by new synthesis. Apparent photoinactivation of catalase has to be regarded as an early indication of photodamage in leaves and conceivably enhances its progress.

PMID:
3800386
DOI:
10.1016/0003-9861(86)90365-6
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center