Sensitized photooxidation of low spin horseradish peroxidase

Journal Article · Sat Jan 01 00:00:00 EST 1977 · Biochem. Biophys. Res. Commun.; (United States)

DOI:https://doi.org/10.1016/0006-291X(77)91640-0· OSTI ID:7076092

Kang, Y J; Spikes, J D

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), Vol. 74:3
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
ENZYMES
INACTIVATION
PEROXIDASES
OXIDATION
PHOTOCHEMICAL REACTIONS
ABSORPTION SPECTROSCOPY
AMINO ACIDS
CHELATES
CYANIDES
EOSIN
HEME
HISTIDINE
HYDROXYL RADICALS
IRON
ISOALLOXAZINES
METHYLENE BLUE
TYROSINE
VISIBLE RADIATION
AMINES
AZINES
AZOLES
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
CHLORIDES
CHLORINE COMPOUNDS
COMPLEXES
DRUGS
DYES
ELECTROMAGNETIC RADIATION
ELEMENTS
HALIDES
HALOGEN COMPOUNDS
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HYDROXY ACIDS
IMIDAZOLES
INDICATORS
METALS
ORGANIC ACIDS
ORGANIC BROMINE COMPOUNDS
ORGANIC COMPOUNDS
ORGANIC HALOGEN COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
ORGANIC OXYGEN COMPOUNDS
ORGANIC SULFUR COMPOUNDS
OXIDOREDUCTASES
PHENOTHIAZINES
PIGMENTS
PORPHYRINS
RADIATIONS
RADICALS
SPECTROSCOPY
TRANSITION ELEMENTS
550200* - Biochemistry