A study of the oxidized form of Pseudomonas aeruginosa cytochrome c-551 peroxidase with the use of magnetic circular dichroism

Abstract
The magnetic properties at different temperatures of oxidized P. aeruginosa cytochrome c-551 peroxidase were studied, with the use of the technique of magnetic-circular-dichroism spectroscopy. At 4.2.degree. K, both constituent hemes were low-spin, and the axial ligand pairs were identified as histidine-histidine and histidine-methionine. At room temperature high-spin signals were observed, amounting to < 25% of the total heme present. These signals are concluded to arise mainly from a temperature-dependent spin-state equilibrium in the methionine-ligated heme.

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