PHOTOINACTIVATION OF CATALASE |
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| Authors: | Lydia Cheng E. W. Kellogg III Lester Packer |
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| Affiliation: | Membrane Bioenergetics Group, Energy and Environment Division, Lawrence Berkeley Laboratory and Department of Physiology/Anatomy, University of California, Berkeley, CA 94720, USA |
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| Abstract: | Abstract— Inactivation of catalase with visible light (>400nm) has been studied in purified bovine liver catalase and in peroxisomal catalase in the mitochondrial fraction of rat liver. Light corresponding to that of maximal absorbance of the heme site (405 nm) was most effective in inactivation. Although photoinactivation is O2 dependent, scavengers of OH radical, 1O2 and O−2 did not protect against loss of activity in either system. Superoxide dismutase partially protected purified catalase added into the mitochondrial fraction system. However, complete protection of catalase was afforded by low concentrations of substrates such as formic acid or methanol which rapidly convert Compound I to Ferricatalase. |
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