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Title: A study of the oxidized form of Pseudomonas aeruginosa cytochrome c-551 peroxidase with the use of magnetic circular dichroism. Author: Foote N, Peterson J, Gadsby PM, Greenwood C, Thomson AJ. Journal: Biochem J; 1984 Oct 15; 223(2):369-78. PubMed ID: 6093773. 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.[Abstract] [Full Text] [Related] [New Search]