The generation of a hyperporphyrin spectrum upon thiol binding to ferric chloroperoxidase. Further evidence of endogenous thiolate ligation to the ferric enzyme.
Open Access
- 1 November 1984
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 259 (21) , 13209-13216
- https://doi.org/10.1016/s0021-9258(18)90679-4
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- A kinetic study of the binding of carbon monoxide to ferrous chloroperoxidaseBiochemistry, 1982
- Models for ferric cytochrome P450. Characterization of hemin mercaptide complexes by electronic and ESR spectraJournal of Inorganic Biochemistry, 1979
- Equilibria between Horseradish Peroxidase and Aromatic Donors.Acta Chemica Scandinavica, 1978
- On the mechanism of compound I formation from peroxidases and catalasesJournal of Theoretical Biology, 1977
- Hyperporphyrin spectra of ferric dimercaptide-hemin complexes. Models for ferric cytochrome P450-thiol complexesJournal of the American Chemical Society, 1977
- Origin of the anomalous Soret spectra of carboxycytochrome P-450Journal of the American Chemical Society, 1976
- 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
- Optical, NMR and EPR properties of horseradish peroxidase and its donor complexesFEBS Letters, 1975
- Moessbauer investigations of chloroperoxidase and its halide complexesBiochemistry, 1973