Reaction of Lactoperoxidase Compound I with Halides and Thiocyanate
Author:
Affiliation:
1. Institute of Chemistry, University of Agricultural Sciences, Muthgasse 18, A-1190 Vienna, Austria, and Institute of Medical Physics and Biophysics, School of Medicine, University of Leipzig, Liebigstrasse 27, D-04103 Leipzig, Germany
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi026326x
Reference36 articles.
1. Glu375Gln and Asp225Val mutants: about the nature of the covalent linkages between heme group and apo-Protein in bovine lactoperoxidase
2. Asp-225 and Glu-375 in Autocatalytic Attachment of the Prosthetic Heme Group of Lactoperoxidase
3. Biochemical Evidence for Heme Linkage through Esters with Asp-93 and Glu-241 in Human Eosinophil Peroxidase
4. Role of Heme in Intracellular Trafficking of Thyroperoxidase and Involvement of H2O2 Generated at the Apical Surface of Thyroid Cells in Autocatalytic Covalent Heme Binding
5. X-ray Crystal Structure and Characterization of Halide-binding Sites of Human Myeloperoxidase at 1.8 Å Resolution
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