{'fraction_non_alphanumeric': 0.01875901875901876, 'fraction_numerical': 0.008658008658008658, 'mean_word_length': 6.261780104712042, '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}}
CATALASE INACTIVATION FOLLOWING PHOTOSENSITIZATION WITH TETRASULFONATEDMETALLOPHTHALOCYANINES

Abstract— Catalase (CAT) in solution or incorporated in erythrocytes and K562 leukemic cells is inactivated during photosensitization with tetrasulfonated metallophthalocyantnes (MePcS4). The effect of added scavengers and D20 showed that both singlet oxygen and free radical species are involved in this process. Evidence was found that direct interactions of ground or excited‐stated photosensitizers with CAT are not responsible for CAT inactivation. Specific techniques to probe early damage to the CAT structure involved optical and EPR spectroscopy, HPLC and polyacrylamide gel electrophoresis analyses. Different primary events of photosensitized protein damage included oxidation of cysteine residues as well as other amino acids, as demonstrated by the formation of carbon‐centered free radicals and the loss of absorbance at λ= 275 nm. In parallel, we detected degradation of the CAT heme groups, accompanied by release of Fe(II) ions in solution. These combined phenomena initiate cross‐linkages between CAT subunits and subsequent degradation of the protein with formation of irreversible aggregates in solution. Phthalocyanine‐mediated photoinactivation of cell‐bound CAT results in loss of protection against accumulating H202, providing an additional pathway of phototoxicity.