Sensitized photooxidation of low spin horseradish peroxidase
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.
- Research Organization:
- Univ. of Utah, Salt Lake City
- OSTI ID:
- 7076092
- Journal Information:
- Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 74:3; ISSN BBRCA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
ABSORPTION SPECTROSCOPY
AMINES
AMINO ACIDS
AZINES
AZOLES
CARBOXYLIC ACIDS
CHELATES
CHEMICAL REACTIONS
CHLORIDES
CHLORINE COMPOUNDS
COMPLEXES
CYANIDES
DRUGS
DYES
ELECTROMAGNETIC RADIATION
ELEMENTS
ENZYMES
EOSIN
HALIDES
HALOGEN COMPOUNDS
HEME
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HISTIDINE
HYDROXY ACIDS
HYDROXYL RADICALS
IMIDAZOLES
INACTIVATION
INDICATORS
IRON
ISOALLOXAZINES
METALS
METHYLENE BLUE
ORGANIC ACIDS
ORGANIC BROMINE COMPOUNDS
ORGANIC COMPOUNDS
ORGANIC HALOGEN COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
ORGANIC OXYGEN COMPOUNDS
ORGANIC SULFUR COMPOUNDS
OXIDATION
OXIDOREDUCTASES
PEROXIDASES
PHENOTHIAZINES
PHOTOCHEMICAL REACTIONS
PIGMENTS
PORPHYRINS
RADIATIONS
RADICALS
SPECTROSCOPY
TRANSITION ELEMENTS
TYROSINE
VISIBLE RADIATION