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- W2034255062 abstract "Metalloporphyrin inhibitors of heme oxygenase may also have photosensitizing properties in vivo. To assess photoactivity in serum, the relative ability to mediate photooxidation of tryptophan or other oxidizable targets, presumably by singlet oxygen production, was measured for tin mesopor-phyrin, zinc mesoporphyrin, and zinc deuteroporphyrin bisglycol in aqueous solution and when bound to human serum albumin. While tin mesoporphyrin sensitized at the greatest initial rate in aqueous solution, the zinc compounds sensitized at a greater initial rate in detergent micelles or when bound to albumin. There was minimal alteration of the tin mesoporphyrin during the time course of illumination in the Soret or visible absorption regions. The zinc compounds, however, proved to be extremely photolabile and were extensively destroyed by light; the photooxidized forms were found to be ineffective as inhibitors of heme oxygenase." @default.
- W2034255062 created "2016-06-24" @default.
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- W2034255062 date "1991-08-01" @default.
- W2034255062 modified "2023-10-18" @default.
- W2034255062 title "COMPARATIVE PHOTO ACTIVITY OF TIN and ZINC PORPHYRIN INHIBITORS OF HEME OXYGENASE: PRONOUNCED PHOTOLABILITY OF THE ZINC COMPOUNDS" @default.
- W2034255062 doi "https://doi.org/10.1111/j.1751-1097.1991.tb02005.x" @default.
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