Heme active-site structural characterization of chloroperoxidase by resonance Raman spectroscopy.
Open Access
- 1 March 1993
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 268 (9), 6189-6193
- https://doi.org/10.1016/s0021-9258(18)53237-3
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- Observation of the FeIV=O stretching Raman band for a thiolate‐ligated heme protein Compound I of chloroperoxidaseFEBS Letters, 1992
- Electron paramagnetic resonance investigations of exogenous ligand complexes of low-spin ferric chloroperoxidase: Further support for endogenous thiolate ligation to the heme ironBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- High-resolution crystal structure of cytochrome P450camJournal of Molecular Biology, 1987
- Raman and infrared spectra of cytochrome c peroxidase-carbon monoxide adducts in alternative conformational statesBiochemistry, 1986
- Alternative carbon monoxide binding modes for horseradish peroxidase studied by resonance Raman spectroscopyBiochemistry, 1986
- Resonance Raman studies of isotopically labeled chloroperoxidaseBiochemistry, 1986
- Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes and proteinsJournal of the American Chemical Society, 1982
- Resonance raman studies of hepatic microsomal cytochromes P-450: evidence for strong .pi. basicity of the fifth ligand in the reduced and carbonyl complex formsBiochemistry, 1978
- Moessbauer investigations of high-spin ferrous heme proteins. II. Chloroperoxidase, horseradish peroxidase, and hemoglobinBiochemistry, 1975
- Moessbauer investigations of chloroperoxidase and its halide complexesBiochemistry, 1973