GLU 242;MET 243(Heme);HIS 336(Heme iron);THR 168;PHE 170;ASP 172;SER 174(Calcium)
Preliminary crystallographic analysis of human myeloperoxidase.
Tetragonal crystals of canine myeloperoxidase suitable for X-ray structural analysis.
Crystallization and subunit structure of canine myeloperoxidase.
Site-directed mutants of human myeloperoxidase. A topological approach to the heme-binding site.
X-ray crystal structure of canine myeloperoxidase at 3 A resolution.
Site-directed mutagenesis of human myeloperoxidase: further identification of residues involved in catalytic activity and heme interaction.
Peroxidasin: a novel enzyme-matrix protein of Drosophila development.
Optical spectrum of myeloperoxidase. Origin of the red shift.
Aromatic substrate molecules bind at the distal heme pocket of myeloperoxidase.
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 167-744
Structure of the green heme in myeloperoxidase.
2.3 A resolution X-ray crystal structure of the bisubstrate analogue inhibitor salicylhydroxamic acid bound to human myeloperoxidase: a model for a prereaction complex with hydrogen peroxide.
Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. Mechanistic studies identifying labile intermediates along the reaction pathway.
The primary and higher order structures of sea urchin ovoperoxidase as determined by cDNA cloning and predicted by homology modeling.
Spin trapping and protein cross-linking of the lactoperoxidase protein radical.
Purification and cloning of the salivary peroxidase/catechol oxidase of the mosquito Anopheles albimanus.
Effects of pH and chloride concentration on resonance Raman spectra of human myeloperoxidase and Raman microspectroscopic analysis of enzyme state in azurophilic granules.
Enzyme-mediated dialdehyde formation: an alternative pathway for benzo[a]pyrene 7,8-dihydrodiol bioactivation.
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 167-744
X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
Impact of missense mutations on biosynthesis of myeloperoxidase.
Internalization of proteinase 3 is concomitant with endothelial cell apoptosis and internalization of myeloperoxidase with generation of intracellular oxidants.
Mutations affecting the calcium-binding site of myeloperoxidase and lactoperoxidase.
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 167-744
Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution.
A transient kinetic study on the reactivity of recombinant unprocessed monomeric myeloperoxidase.
This enzyme is composed of light chain (chain A or B in PDB) and heavy chain (chain C or D in PDB). Although this enzyme binds a calcium ion, it is not directly involved in catalysis.