Oxidation of 1,2,4,5-tetramethoxybenzene by lignin peroxidase of Phanerochaete chrysosporium.
Identifieur interne : 000C37 ( Main/Exploration ); précédent : 000C36; suivant : 000C38Oxidation of 1,2,4,5-tetramethoxybenzene by lignin peroxidase of Phanerochaete chrysosporium.
Auteurs : R S Koduri [États-Unis] ; R E Whitwam ; D. Barr ; S D Aust ; M. TienSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 1996.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Anisoles.
- enzymologie : Basidiomycota.
- métabolisme : Anisoles, Peroxidases.
- Cations, Cinétique, Oxydoréduction, Radicaux libres, Spécificité du substrat.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Anisoles.
- chemical , metabolism : Anisoles, Peroxidases.
- enzymology : Basidiomycota.
- chemical : Cations, Free Radicals, Kinetics, Oxidation-Reduction, Substrate Specificity.
Abstract
We have reinvestigated the lignin peroxidase-catalyzed oxidation of 1,2,4,5-tetramethoxybenzene (TMB) by using presteady-state and steady-state kinetic methods. Our presteady-state kinetic results show that the reaction of compound I with TMB obeyed second order kinetics with a rate constant of 1.1 x 10(7) M-1s-1. The reaction of compound II with TMB exhibits a hyperbolic concentration dependence with a Kd of 16 microM and K = 24 s-1. The stoichiometry of TMB oxidation during steady state is two TMB cation radicals formed per H2O2 consumed. These results clearly show that TMB is a good substrate for both compounds I and II of lignin peroxidase.
DOI: 10.1006/abbi.1996.0074
PubMed: 8611032
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Our presteady-state kinetic results show that the reaction of compound I with TMB obeyed second order kinetics with a rate constant of 1.1 x 10(7) M-1s-1. The reaction of compound II with TMB exhibits a hyperbolic concentration dependence with a Kd of 16 microM and K = 24 s-1. The stoichiometry of TMB oxidation during steady state is two TMB cation radicals formed per H2O2 consumed. These results clearly show that TMB is a good substrate for both compounds I and II of lignin peroxidase.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8611032</PMID><DateCompleted><Year>1996</Year><Month>05</Month><Day>24</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>14</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-9861</ISSN><JournalIssue CitedMedium="Print"><Volume>326</Volume><Issue>2</Issue><PubDate><Year>1996</Year><Month>Feb</Month><Day>15</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Oxidation of 1,2,4,5-tetramethoxybenzene by lignin peroxidase of Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>261-5</MedlinePgn></Pagination><Abstract><AbstractText>We have reinvestigated the lignin peroxidase-catalyzed oxidation of 1,2,4,5-tetramethoxybenzene (TMB) by using presteady-state and steady-state kinetic methods. Our presteady-state kinetic results show that the reaction of compound I with TMB obeyed second order kinetics with a rate constant of 1.1 x 10(7) M-1s-1. The reaction of compound II with TMB exhibits a hyperbolic concentration dependence with a Kd of 16 microM and K = 24 s-1. The stoichiometry of TMB oxidation during steady state is two TMB cation radicals formed per H2O2 consumed. 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Barr</name><name sortKey="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. Tien</name><name sortKey="Whitwam, R E" sort="Whitwam, R E" uniqKey="Whitwam R" first="R E" last="Whitwam">R E Whitwam</name></noCountry><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Koduri, R S" sort="Koduri, R S" uniqKey="Koduri R" first="R S" last="Koduri">R S Koduri</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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