| Literature DB >> 3986209 |
A J Sitter, C M Reczek, J Terner.
Abstract
We have directly observed the oxyferryl group of ferryl myoglobin by resonance Raman spectroscopy. The FeIV = O stretching vibration is observed at 797 cm-1 and confirmed by an 18O-induced isotopic shift to 771 cm-1. The porphyrin center-to-nitrogen distance of ferryl myoglobin is significantly less than that previously observed for horseradish peroxidase compound II, which also contains an FeIV = O heme. The FeIII-CN- stretch of myoglobin (FeIII) cyanide is observed at 454 cm-1, which shifts to 449 cm-1 upon substitution with [13C]cyanide.Entities:
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Year: 1985 PMID: 3986209 DOI: 10.1016/0167-4838(85)90301-2
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002