Title : Studies of the radical species in compound ES of cytochrome c peroxidase altered by site-directed mutagenesis.

Pub. Date : 1986 Mar

PMID : 3006043






4 Functional Relationships(s)
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1 Yeast cytochrome c peroxidase reacts with hydrogen peroxide to form an intermediate, compound ES, in which the heme iron atom is converted to a ferryl function (Fe4+ = O) and a radical center is generated on a reversibly oxidizable amino acid residue of uncertain identity. Hydrogen Peroxide cytochrome-c peroxidase Saccharomyces cerevisiae S288C
2 Yeast cytochrome c peroxidase reacts with hydrogen peroxide to form an intermediate, compound ES, in which the heme iron atom is converted to a ferryl function (Fe4+ = O) and a radical center is generated on a reversibly oxidizable amino acid residue of uncertain identity. Heme cytochrome-c peroxidase Saccharomyces cerevisiae S288C
3 Yeast cytochrome c peroxidase reacts with hydrogen peroxide to form an intermediate, compound ES, in which the heme iron atom is converted to a ferryl function (Fe4+ = O) and a radical center is generated on a reversibly oxidizable amino acid residue of uncertain identity. Iron cytochrome-c peroxidase Saccharomyces cerevisiae S288C
4 As methionine-172 is a possible site of this radical, we have constructed specific variants of cytochrome c peroxidase in which methionine-172 is replaced by serine or cysteine. Methionine cytochrome-c peroxidase Saccharomyces cerevisiae S288C