Electron-paramagnetic-resonance studies on a photochemically produced species of horseradish peroxidase compound I
- 1 October 1977
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 167 (1) , 31-37
- https://doi.org/10.1042/bj1670031
Abstract
Strong electron-paramagnetic-resonance signals in the g = 2.00 region were detected after irradiation of horseradish peroxidase Compound I at temperatures of 10 and 100 K. These signals establish the presence of new free-radical species in the peroxidase system. The new species are interpreted in terms of a haem-photosensitized oxidation of the protein's peptide groups close to the Compound I radical site. On warming to room temperature, the radicals decayed irreversibly to a species having a weak asymmetric electron-paramagnetic-resonance signal at 100 K, which could still be observed after incubation at room temperature for more than 1 h.This publication has 20 references indexed in Scilit:
- Nature of the free radical in ribonucleotide reductase from Escherichia coli.Journal of Biological Chemistry, 1977
- Horseradish peroxidase. XXV. An electron spin resonance study of the low temperature photochemical reaction of Compound IBiochemical and Biophysical Research Communications, 1977
- Characterization of the chromophores in horseradish peroxidase compounds I and II using magnetic circular dichroismBiochemical and Biophysical Research Communications, 1976
- Photosensitization of small peptides by proflavine: An E.S.R. study at low temperatureRadiation and Environmental Biophysics, 1974
- [Electron paramagnetic resonance spectra of ribonuclease, photosensitized with proflavine].1972
- Interaction of peroxidases with aromatic peracids and alkyl peroxides. Product analysis.1972
- Primary compounds of catalase and peroxidaseBiochemical Journal, 1961
- Magnetic properties of some peroxide compounds of myoglobin, peroxidase and catalaseArchives of Biochemistry and Biophysics, 1952
- The spectra of the enzyme-substrate complexes of catalase and peroxidaseArchives of Biochemistry and Biophysics, 1952
- Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobinBiochemical Journal, 1951