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Published on: June 27, 2014
Resonance Raman spectroscopy of soybean peroxidase
1Department of Chemistry, Northeastern University, Boston, Massachusetts 02115, USA.
Abstract:
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.
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