Broad-line nuclear magnetic resonance studies of chloroperoxidase.
Chloroperoxidase, a heme glycoprotein isolated from the mold Caldariomyces fumago, was studied by NMR relaxation techniques. Interaction of the chloride ion substrate with the enzyme may be analyzed as consisting of at least three contributions: a weak interaction with the iron atom, nonspecific anion-protein interactions, and a specific interaction generated at low pH. The data indicate that a specific interaction, which develops in parallel with enzyme activity at low pH, does not occur at the iron atom first coordination sphere site. The results are summarized in terms of an enzymatic mechanism not involving chloride ion coordination to the iron atom.
D001665:Binding Sites; D002712:Chlorides / Q000494:pharmacology; D005459:Fluorides / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D003904:Mitosporic Fungi / Q000201:enzymology*; D010544:Peroxidases / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation
D002712:Chlorides; D010544:Peroxidases; D005459:Fluorides