Asp-225 and Glu-375 in Autocatalytic Attachment of the Prosthetic Heme Group of Lactoperoxidase
Open Access
- 1 March 2002
- journal article
- Published by Elsevier
- Vol. 277 (9), 7191-7200
- https://doi.org/10.1074/jbc.m109523200
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- X-ray Crystal Structure and Characterization of Halide-binding Sites of Human Myeloperoxidase at 1.8 Å ResolutionJournal of Biological Chemistry, 2000
- The Sulfonium Ion Linkage in MyeloperoxidaseJournal of Biological Chemistry, 1999
- Biochemical Evidence for Heme Linkage through Esters with Asp-93 and Glu-241 in Human Eosinophil PeroxidaseJournal of Biological Chemistry, 1999
- The Heme Prosthetic Group of LactoperoxidasePublished by Elsevier ,1998
- Difference Fourier Transform Infrared Evidence for Ester Bonds Linking the Heme Group in Myeloperoxidase, Lactoperoxidase, and Eosinophil PeroxidaseJournal of the American Chemical Society, 1997
- Autocatalytic Processing of Heme by Lactoperoxidase Produces the Native Protein-bound Prosthetic GroupPublished by Elsevier ,1997
- A theoretical three-dimensional model for lactoperoxidase and eosinophil peroxidase, built on the scaffold of the myeloperoxidase X-ray structureJBIC Journal of Biological Inorganic Chemistry, 1996
- Lactoperoxidase Heme Structure Characterized by Paramagnetic Proton NMR SpectroscopyJournal of the American Chemical Society, 1996
- Structure of the Green Heme in MyeloperoxidaseArchives of Biochemistry and Biophysics, 1995
- Isolation and Identification of a Protoheme IX Derivative Released During Autolytic Cleavage of Human MyeloperoxidaseArchives of Biochemistry and Biophysics, 1995