title: Resonance Raman studies of isotopically labeled chloroperoxidase.
abstract: Chloroperoxidase (CPO) and cytochrome P450cam have been shown by several techniques to have similar active site properties. Recent resonance Raman investigations using isotopically enriched 34S-labeled samples have demonstrated thiolate ligation in the P450cam system. We report here on a number of parallel studies involving CPO. On the basis of isotopic labeling (34S, 13CO), we assign the Fe-S and Fe-CO stretching frequencies of CPO at 347 (-vFe-S) and 488 cm-1 (-vFe-CO). The differences of the -vFe-S and -vFe-CO in CPO and P450cam may suggest subtle differences in the thiolate binding in the two systems.
mesh_terms: D002711:Chloride Peroxidase / Q000378:metabolism*; D007700:Kinetics; D003904:Mitosporic Fungi / Q000201:enzymology / Q000254:growth & development; D010544:Peroxidases / Q000378:metabolism*; D013059:Spectrum Analysis, Raman / Q000379:methods; D013431:Sulfates / Q000378:metabolism; D013462:Sulfur Radioisotopes
chemical_list: D013431:Sulfates; D013462:Sulfur Radioisotopes; D010544:Peroxidases; D002711:Chloride Peroxidase