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. 1984 Oct 15;223(2):369-78.
doi: 10.1042/bj2230369.

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

N Foote, J Peterson, P M Gadsby, C Greenwood, A J Thomson

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

N Foote et al. Biochem J. .

Abstract

The magnetic properties at different temperatures of oxidized Pseudomonas aeruginosa cytochrome c-551 peroxidase were studied, with the use of the technique of magnetic-circular-dichroism spectroscopy. At 4.2K, both constituent haems were found to be 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 less than 25% of the total haem present. These signals are concluded to arise mainly from a temperature-dependent spin-state equilibrium in the methionine-ligated haem.

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