Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex.
Identifieur interne : 000B95 ( Main/Corpus ); précédent : 000B94; suivant : 000B96Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex.
Auteurs : A. Khindaria ; G. Nie ; S D AustSource :
- Biochemistry [ 0006-2960 ] ; 1997.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Benzyl Alcohols, Hemeproteins, Isoenzymes, Peroxidases.
- enzymology : Basidiomycota.
- chemical : Cations, Cold Temperature, Electron Spin Resonance Spectroscopy, Free Radicals.
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 pi 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 perpendicular only marginally greater than g parallel. 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 parallel greater than g perpendicular. 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.
DOI: 10.1021/bi9715730
PubMed: 9369491
Links to Exploration step
pubmed:9369491Le document en format XML
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<author><name sortKey="Khindaria, A" sort="Khindaria, A" uniqKey="Khindaria A" first="A" last="Khindaria">A. Khindaria</name>
<affiliation><nlm:affiliation>Biotechnology Center, Utah State University, Logan, Utah 84322-4705, USA.</nlm:affiliation>
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<author><name sortKey="Nie, G" sort="Nie, G" uniqKey="Nie G" first="G" last="Nie">G. Nie</name>
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<author><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term>
<term>Benzyl Alcohols (metabolism)</term>
<term>Cations (MeSH)</term>
<term>Cold Temperature (MeSH)</term>
<term>Electron Spin Resonance Spectroscopy (MeSH)</term>
<term>Free Radicals (MeSH)</term>
<term>Hemeproteins (metabolism)</term>
<term>Isoenzymes (metabolism)</term>
<term>Peroxidases (metabolism)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Benzyl Alcohols</term>
<term>Hemeproteins</term>
<term>Isoenzymes</term>
<term>Peroxidases</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Cations</term>
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<front><div type="abstract" xml:lang="en">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 pi 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 perpendicular only marginally greater than g parallel. 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 parallel greater than g perpendicular. 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.</div>
</front>
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<DateRevised><Year>2012</Year>
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<Issue>46</Issue>
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<Title>Biochemistry</Title>
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<ArticleTitle>Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex.</ArticleTitle>
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<Abstract><AbstractText>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 pi 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 perpendicular only marginally greater than g parallel. 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 parallel greater than g perpendicular. 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.</AbstractText>
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