Electrolysis-mediated irreversible inactivation of lipoxygenase directed toward electroaffinity labelling.
Irreversible inhibition of soybean lipoxygenase-1 ( SL-1) was accomplished via a controlled potential oxidative electrolysis of 1,5-dihydroxynaphthalene (1,5-DHN) at +0.8 V vs SCE. The inactivation of SL-1 with this known inhibitor was greatly enhanced under these electrolytic conditions to which the enzyme itself was stable. Electrolyses were run at 0 degree C in a 0.05 M phosphate buffer, pH 7.0, using graphite cloth electrodes. The rate of inactivation was observed to be limited by and dependent on the anodic oxidation of 1,5-DHN. The non-oxidizable (at this potential) inhibitor indomethacin was shown to protect the enzyme from irreversible inactivation, however, an external nucleophile (2-mercaptoethanol) had little effect. These initial studies support the capability of such electrochemical methods for the site-specific covalent modification (affinity labelling) of lipoxygenase, and perhaps other enzymes.[1]References
- Electrolysis-mediated irreversible inactivation of lipoxygenase directed toward electroaffinity labelling. Holmes, T.J., Vennerstrom, J.L., John, V. Biochem. Biophys. Res. Commun. (1984) [Pubmed]
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