Abstract
A number of 57 Fe enriched peroxidase and its derivatives are investigated by the Mössbauer effect of heme-iron. Fluoride compound exhibited broad magnetic hyperfine splittings characteristic of ferric high-spin state. Hydroxide and azide compounds showed large quadrupole splittings resulting from ferric low-spin states. Free peroxidase and cyanide compound exhibited quadrupole splittings of strong temperature dependence. The temperature dependence of quadrupole splittings is too strong to be ascribed to ( d ε ) 5 state. The small quadrupole splitting and small isomer shift of cyanide compound are attributable to the covalent mixing of CN - and ferriciron. The reduced peroxidase exhibited large isomer shift and large quadrupole splitting of strong temperature dependence. These are the characteristics of ferrous high-spin state. Reduced carbon monoxide compound showed a small quadrupole splitting, which is attributable to ferrous low-spin state.
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