{'fraction_non_alphanumeric': 0.018018018018018018, 'fraction_numerical': 0.0, 'mean_word_length': 5.864197530864198, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Mechanistic studies of tyrosinase suicide inactivation

Tyrosinase is a copper containing enzyme that oxidises both phenols and catechols to ortho- quinones. The oxidation of catechols (oxidase activity) is associated with a gradual and irreversible inactivation of the enzyme. This suicide inactivation has been interpreted in terms of the enzyme occasionally oxidising catechols as phenols (oxygenase activity) leading to reductive elimination of copper. In this account experimental evidence supporting the authors' mechanism is reviewed and discussed.