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EVIDENCE AGAINST THE PRODUCTION OF SUPEROXIDE BY PHOTOIRRADIATION OF HEMATOPORPHYRIN DERIVATIVE
Author(s) -
Gibson Scott L.,
Cohen Harvey J.,
Hilf Russell
Publication year - 1984
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1984.tb04615.x
Subject(s) - hematoporphyrin , adrenochrome , chemistry , superoxide , methylene blue , xanthine oxidase , cytochrome c , oxidase test , photochemistry , cytochrome c oxidase , cytochrome , oxygen , medicinal chemistry , biochemistry , mitochondrion , photodynamic therapy , enzyme , epinephrine , organic chemistry , biology , catalysis , photocatalysis , endocrinology
Experiments were performed to ascertain whether superoxide anion (O 2 − ) was produced by the photodynamic activation of hematoporphyrin derivative (HPD). Three different systems were utilized to detect formation of O 2 − , oxidation of epinephrine to adrenochrome, reduction of cytochrome c and reduction of nitro blue tetrazolium (NBT). The effects on these detectors under identical conditions for HPD + h ν were compared to those obtained with two O 2 − generating systems, riboflavin + by and xanthine‐xanthine oxidase, and to a singlet oxygen generating system, photoradiation of methylene blue. The results indicated that HPD + hv differed from the two O 2 − generating systems in failing to reduce cytochrome c or NET, and that HPD + h ν was similar to the behavior of methylene blue + h ν . In addition, HPD + h ν but not the O 2 − generating systems could inhibit mitochondrial cytochrome c oxidase activity. We conclude that the photodynamic activation of HPD does not produce O 2 − as a major oxygen radical and that the effects of HPD + h ν on mitochondrial cytochrome c oxidase are not caused by O 2 − .