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- W2023784133 abstract "Lignin peroxidases (LiP) from the white-rot fungus Phanerochaete chrysosporium oxidize veratryl alcohol (VA) by two electrons to veratryl aldehyde, although the VA cation radical (VA•+) is an intermediate [Khindaria, A., et al. (1995) Biochemistry 34, 6020−6025]. It was speculated, on the basis of kinetic evidence, that VA•+ can form a catalytic complex with LiP compound II. We have used low-temperature EPR to provide direct evidence for the formation of the complex. The EPR spectrum of VA•+ obtained at 4 K was explained by a model for coupling between the oxoferryl moiety of the heme (S = 1) and VA•+ (S = 1/2) similar to the model proposed for an oxyferryl and a porphyrin π cation radical of horseradish peroxidase. The coupling constant suggested that VA•+ was equally ferro- and antiferromagnetically coupled to the oxoferryl moiety. The spectrum was simulated with g⊥ only marginally greater than g∥. This was surprising since the only other known organic radical coupled to the heme iron in a peroxidase is the tryptophan cation radical in cytochrome c peroxidase which exhibits a g tensor with g∥ greater than g⊥. Spin concentration analysis suggested that the 1 mol of VA•+ was coupled to the oxoferryl moiety per mole of enzyme. The VA•+ signal decayed with a first-order decay constant of 1.76 s-1, in close agreement with the earlier published decay constant of 1.85 s-1 from room-temperature EPR studies. The exchange coupling between VA•+ and the oxoferryl moiety strongly advocates calling this species (VA•+ and LiP compound II) a catalytic complex." @default.
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- W2023784133 date "1997-11-01" @default.
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- W2023784133 title "Detection and Characterization of the Lignin Peroxidase Compound II−Veratryl Alcohol Cation Radical Complex" @default.
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- W2023784133 doi "https://doi.org/10.1021/bi9715730" @default.
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