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- W2078695988 abstract "Horseradish peroxidase differs from most enzymes in that it is almost completely resistant to photodynamic action due to the paramagnetic ferric ion in the prosthetic group, heme. Chelation of horseradish peroxidase at the sixth coordination position of the iron with a cyanide or hydroxyl group converts it to a low spin diamagnetic state. Upon illumination with visible light with eosin Y, flavin mononucleotide or methylene blue as sensitizer, the low spin enzyme lost both peroxidative and oxidative activities with the same quantum yields. Several amino acid residues, including one histidine and one tyrosine were destroyed in the low spin enzyme after 60 min of illumination with eosin Y as sensitizer." @default.
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- W2078695988 date "1977-02-01" @default.
- W2078695988 modified "2023-09-27" @default.
- W2078695988 title "Sensitized photooxidation of low spin horseradish peroxidase" @default.
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- W2078695988 doi "https://doi.org/10.1016/0006-291x(77)91640-0" @default.
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