Resonance Raman evidence for the activation of dioxygen in horseradish oxyperoxidase.
Resonance Raman spectroscopy has been employed to investigate the molecular bases for the markedly different properties of horseradish oxyperoxidase and oxymyoglobin. The porphyrin core of oxyperoxidase is slightly more expanded with the iron atom closer to the porphyrin plane, and there is greater iron d pi-to-oxygen pi backbonding compared to oxymyoglobin. The iron-oxygen (stretching or bending) bands are observed at 570 and 562 cm-1, respectively, for oxymyoglobin and oxyperoxidase, and the iron-His stretching bands have been tentatively identified at 276 and 289 cm-1, respectively. It is suggested that the stronger iron-His bond in oxyperoxidase facilitates greater iron d pi-to-oxygen pi backdonation by raising the energy of the iron d pi orbitals closer to the energy of the oxygen pi orbitals. This weakens the O-O bond and activates dioxygen for use as an electron acceptor in the peroxidase-oxidase reaction.
D006735:Horseradish Peroxidase / Q000378:metabolism*; D007501:Iron; D009211:Myoglobin / Q000378:metabolism; D010100:Oxygen / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D013059:Spectrum Analysis, Raman
D009211:Myoglobin; C017595:oxymyoglobin; D007501:Iron; D006735:Horseradish Peroxidase; D010544:Peroxidases; D010100:Oxygen