Resonance Raman spectroscopy of soybean peroxidase.
Resonance Raman spectra (600-1700 cm-1) for the heme enzyme soybean peroxidase (Rz = 2.5) were obtained using Soret band excitation at 406.7 nm. The vibrational frequencies and depolarization data indicate a strong similarity between the active sites of soybean and horseradish peroxidase. This similarity suggests that the active site in the resting form of soybean peroxidase contains a ferric iron, is a high-spin 5-coordinate heme binding His as a fifth axial ligand.
Bedard
P
P
Department of Chemistry, Northeastern University, Boston, Massachusetts 02115, USA.
Mabrouk
P A
PA
D001665:Binding Sites; D006735:Horseradish Peroxidase / Q000737:chemistry; D007527:Isoenzymes / Q000737:chemistry; D007834:Lasers; D009195:Peroxidase / Q000737:chemistry* / Q000378:metabolism; D013025:Glycine max / Q000201:enzymology*; D013059:Spectrum Analysis, Raman
D007527:Isoenzymes; D006735:Horseradish Peroxidase; D009195:Peroxidase