A possible origin of chemiluminsecence in phagocytosing neutrophils. Myeloperoxidase-mediated chlorination of proteins and tryptophan.
Chlorination of proteins by the myeloperoxidase-H2O2-Cl- system results in light emission. Out of all amino acids present in proteins only tryptophan delivers light during chlorination. Chlorination of tryptophan by the myeloperoxidase-H2O2-Cl- system, as well as by HOCl or taurine chloramine is associated with chemiluminescence. pH dependence and time pattern of light emission is similar for chlorination of tryptophan by the myeloperoxidase system and taurine, but appears to be different for chlorination by HOCl. Aerobic conditions are necessary for chemiluminescence of chlorinated tryptophan.
D002713:Chlorine / Q000378:metabolism*; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008163:Luminescent Measurements; D009504:Neutrophils / Q000276:immunology*; D010587:Phagocytosis; D011506:Proteins / Q000378:metabolism*; D013997:Time Factors; D014364:Tryptophan / Q000378:metabolism
D011506:Proteins; D002713:Chlorine; D014364:Tryptophan; D006861:Hydrogen Peroxide