Resonance Raman evidence for the activation of dioxygen in horseradish oxyperoxidase.
作者： H E Van Wart , J Zimmer
DOI: 10.1016/S0021-9258(17)39483-8
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摘要: Resonance Raman spectroscopy has been employed to investigate the molecular bases for markedly different properties of horseradish oxyperoxidase and oxymyoglobin. The porphyrin core is slightly more expanded with iron atom closer plane, there greater d pi-to-oxygen pi backbonding compared iron-oxygen (stretching or bending) bands are observed at 570 562 cm-1, respectively, oxymyoglobin oxyperoxidase, iron-His stretching have tentatively identified 276 289 respectively. It suggested that stronger bond in facilitates backdonation by raising energy orbitals oxygen orbitals. This weakens O-O activates dioxygen use as an electron acceptor peroxidase-oxidase reaction.
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