Resonance Raman studies of isotopically labeled chloroperoxidase.
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.
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
D013431:Sulfates; D013462:Sulfur Radioisotopes; D010544:Peroxidases; D002711:Chloride Peroxidase