Title : X-ray absorption and resonance raman spectroscopy of human myeloperoxidase at neutral and acid pH.

Pub. Date : 1997 Apr 4

PMID : 9128147






3 Functional Relationships(s)
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1 While MPO shows significant sequence homology with other peroxidases and this homology is particularly striking among the active-site residues, MPO exhibits unusual spectral features and the unique ability to catalyze the oxidation of chloride ions. Chlorides myeloperoxidase Homo sapiens
2 While MPO shows significant sequence homology with other peroxidases and this homology is particularly striking among the active-site residues, MPO exhibits unusual spectral features and the unique ability to catalyze the oxidation of chloride ions. Chlorides myeloperoxidase Homo sapiens
3 This change suggests that loss of the distal ligand in MPO releases stress on the heme which may facilitate binding of chloride ion. Chlorides myeloperoxidase Homo sapiens