Abstract
A number of sulphur ligands in solution with protoporphyrin IX iron(II) give Mössbauer data similar to that recorded for cytochromes P-450 in the deoxy-high-spin ferrous stage. Addition of carbonyl to the solution results in Mössbauer spectra that have wider quadrupole splittings than that of P-450 CO. This suggest that the sulphur to iron bond in the cytochromes P-450 is unusually strong, probably due to other bonding forces in these proteins.
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