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Lignin peroxidase (LiP) from Phanerochaete chrysosporium was purified and subsequently studied in detail with regard to its susceptibility to proteolytic degradation. While LiP is stable under standard conditions, the presence of a series of sulfhydryl-containing compounds (cysteine, cystine, mercaptoethanol, and 2-mercaptoethanol) virtually completely inhibited proteolysis of the enzyme. On the other hand, several thiol-containing compounds with properties similar to those of cysteine, cystine, and 2-mercaptoethanol (e.g., p-chloromercuribenzoate, N-ethylmaleimide, and iodoacetic acid) were found to be highly potent inhibitors of the enzyme. Both inhibition of proteolysis and inactivation of the enzyme were observed in the presence of various thiol-containing compounds. The effect of iodoacetic acid is particularly striking. Within 15 min, more than 80% of the enzymatic activity is lost. A thiol-mediated destruction of the enzyme was also observed when purified LiP was exposed to different concentrations of cysteine and cystine. The formation of free radicals was suggested by the protective effect of catalase and dimethyl sulfoxide. Inhibition of cysteine-mediated inactivation of LiP was also observed with several oxidizable and nonoxidizable transition metals. It is concluded that thiol compounds play a key role in the in ac619d1d87
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