Thiols as peroxidase substrates.

B E Svensson; A Gräslund; G Ström; P Moldeus

doi:10.1016/0891-5849(93)90007-h

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Thiols as peroxidase substrates.

B E Svensson·A Gräslund·G Ström·P Moldeus

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Abstract

The abilities of haem peroxidases to catalyse the oxidation of various thiols were studied using the spin-trapping electron spin resonance (ESR) technique. Myeloperoxidase, a neutrophil and monocyte enzyme, catalysed the oxidation of cysteamine, cysteine methyl, and ethyl ester and to some extent 2-mercaptoethanol and thioglycollic acid. This peroxidase poorly catalysed the oxidation of cysteine, N-acetylcysteine, penicillamine, and glutathione under the same conditions. The dependence on pH of peroxidase-catalysed thiol oxidation may indicate that the thiolate anion form is the actual peroxidase substrate. Another leucocyte peroxidase, eosinophil peroxidase, had similar catalytic properties toward thiols as myeloperoxidase. Lactoperoxidase (found in milk, saliva, and tears) and the plant horseradish peroxidase were, however, different from the aforementioned leucocyte peroxidases in their abilities to catalyse the oxidation of thiols.

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Catalysis Cysteamine Cysteine Electron Spin Resonance Spectroscopy Eosinophil Peroxidase Horseradish Peroxidase Hydrogen-Ion Concentration Lactoperoxidase Mercaptoethanol Peroxidase Peroxidases Substrate Specificity Sulfhydryl Compounds Thioglycolates Comparative Study Journal Article

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B E Svensson, A Gräslund, G Ström, P Moldeus. 1993. Thiols as peroxidase substrates.. https://doi.org/10.1016/0891-5849(93)90007-h

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