An electron paramagnetic resonance study of the high and low spin forms of chloroperoxidase.
Open Access
- 1 May 1980
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 255 (10) , 4801-4807
- https://doi.org/10.1016/s0021-9258(19)85568-0
Abstract
No abstract availableThis publication has 37 references indexed in Scilit:
- Resonance Raman investigations of chloroperoxidase, horseradish peroxidase, and cytochrome c using Soret band laser excitationBiochemistry, 1979
- Origin of the anomalous Soret spectra of carboxycytochrome P-450Journal of the American Chemical Society, 1976
- Ferrous porphyrin-mercaptide complexes. Models for reduced cytochrome P-450Journal of the American Chemical Society, 1975
- Chloroperoxidase. P-450 type absorption in the absence of sulfhydryl groupsBiochemistry, 1975
- Moessbauer investigations of high-spin ferrous heme proteins. II. Chloroperoxidase, horseradish peroxidase, and hemoglobinBiochemistry, 1975
- Model for the carbonyl adduct of ferrous cytochrome P 450Journal of the American Chemical Society, 1975
- Porphyrins. XXXII. Absorptions and luminescence of Cr(III) complexesThe Journal of Chemical Physics, 1975
- Moessbauer investigations of chloroperoxidase and its halide complexesBiochemistry, 1973
- The Molar Light Absorption of Pyridine Ferroprotoporphrin (Pyridine Haemochromogen).Acta Chemica Scandinavica, 1953
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934