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Iodide as the mediator for the reductive reactions of peroxidases.

Identifieur interne : 001E06 ( Main/Exploration ); précédent : 001E05; suivant : 001E07

Iodide as the mediator for the reductive reactions of peroxidases.

Auteurs : M M Shah ; S D Aust

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 1993.

RBID : pubmed:8386162

Descripteurs français

KwdFr :
- Acide édétique (composition chimique), Acide édétique (métabolisme), Basidiomycota (métabolisme), Cytochromes de type c (composition chimique), Cytochromes de type c (métabolisme), Iodures (métabolisme), Myeloperoxidase (métabolisme), Oxydoréduction (MeSH), Radicaux libres (MeSH), Spectroscopie de résonance de spin électronique (MeSH).
MESH :
- composition chimique : Acide édétique, Cytochromes de type c.
- métabolisme : Acide édétique, Basidiomycota, Cytochromes de type c, Iodures, Myeloperoxidase.
- Oxydoréduction, Radicaux libres, Spectroscopie de résonance de spin électronique.

English descriptors

KwdEn :
- Basidiomycota (metabolism), Cytochrome c Group (chemistry), Cytochrome c Group (metabolism), Edetic Acid (chemistry), Edetic Acid (metabolism), Electron Spin Resonance Spectroscopy (MeSH), Free Radicals (MeSH), Iodides (metabolism), Oxidation-Reduction (MeSH), Peroxidase (metabolism).
MESH :
- chemical , chemistry : Cytochrome c Group, Edetic Acid.
- metabolism : Basidiomycota, Cytochrome c Group, Edetic Acid, Iodides, Peroxidase.
- Electron Spin Resonance Spectroscopy, Free Radicals, Oxidation-Reduction.

Abstract

Lignin peroxidase H2 (LiPH2) from the white rot fungus Phanerochaete chrysosporium catalyzed the reduction of cytochrome c, nitro blue tetrazolium, ferric iron, molecular oxygen, and triiodide in a reaction mixture containing LiPH2, H2O2, EDTA, and iodide. Activity followed first order kinetics with respect to EDTA concentration. The reductive activity observed with LiPH2 using iodide as the mediator was comparable to that obtained using a variety of other free radical mediators such as veratryl alcohol, 1,4-dimethoxybenzene, and 1,2,3- and 1,2,4-trimethoxybenzene. EDTA-derived radicals were detected by ESR spin trapping upon incubation of LiPH2 with H2O2, iodide, and EDTA. Reduction activity was also observed using other peroxidases such as lactoperoxidase, horseradish peroxidase, and myeloperoxidase. For the reduction activity of LiPH2, it is proposed that the oxidation of EDTA is mediated by the iodide radical, and the reduction of various electron acceptors is mediated by EDTA radicals. The inhibition of reduction activity at higher concentrations of iodide might be due to the combination of iodide radicals to form I2 which forms a stable triiodide complex by reacting with excess iodide.

PubMed: 8386162

Affiliations:

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Le document en format XML

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<author><name sortKey="Shah, M M" sort="Shah, M M" uniqKey="Shah M" first="M M" last="Shah">M M Shah</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (metabolism)</term>
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<term>Cytochrome c Group (metabolism)</term>
<term>Edetic Acid (chemistry)</term>
<term>Edetic Acid (metabolism)</term>
<term>Electron Spin Resonance Spectroscopy (MeSH)</term>
<term>Free Radicals (MeSH)</term>
<term>Iodides (metabolism)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Peroxidase (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acide édétique (composition chimique)</term>
<term>Acide édétique (métabolisme)</term>
<term>Basidiomycota (métabolisme)</term>
<term>Cytochromes de type c (composition chimique)</term>
<term>Cytochromes de type c (métabolisme)</term>
<term>Iodures (métabolisme)</term>
<term>Myeloperoxidase (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Radicaux libres (MeSH)</term>
<term>Spectroscopie de résonance de spin électronique (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cytochrome c Group</term>
<term>Edetic Acid</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Acide édétique</term>
<term>Cytochromes de type c</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Basidiomycota</term>
<term>Cytochrome c Group</term>
<term>Edetic Acid</term>
<term>Iodides</term>
<term>Peroxidase</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide édétique</term>
<term>Basidiomycota</term>
<term>Cytochromes de type c</term>
<term>Iodures</term>
<term>Myeloperoxidase</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Electron Spin Resonance Spectroscopy</term>
<term>Free Radicals</term>
<term>Oxidation-Reduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Oxydoréduction</term>
<term>Radicaux libres</term>
<term>Spectroscopie de résonance de spin électronique</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Lignin peroxidase H2 (LiPH2) from the white rot fungus Phanerochaete chrysosporium catalyzed the reduction of cytochrome c, nitro blue tetrazolium, ferric iron, molecular oxygen, and triiodide in a reaction mixture containing LiPH2, H2O2, EDTA, and iodide. Activity followed first order kinetics with respect to EDTA concentration. The reductive activity observed with LiPH2 using iodide as the mediator was comparable to that obtained using a variety of other free radical mediators such as veratryl alcohol, 1,4-dimethoxybenzene, and 1,2,3- and 1,2,4-trimethoxybenzene. EDTA-derived radicals were detected by ESR spin trapping upon incubation of LiPH2 with H2O2, iodide, and EDTA. Reduction activity was also observed using other peroxidases such as lactoperoxidase, horseradish peroxidase, and myeloperoxidase. For the reduction activity of LiPH2, it is proposed that the oxidation of EDTA is mediated by the iodide radical, and the reduction of various electron acceptors is mediated by EDTA radicals. The inhibition of reduction activity at higher concentrations of iodide might be due to the combination of iodide radicals to form I2 which forms a stable triiodide complex by reacting with excess iodide.</div>
</front>
</TEI>
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<DateCompleted><Year>1993</Year>
<Month>05</Month>
<Day>14</Day>
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<DateRevised><Year>2013</Year>
<Month>11</Month>
<Day>21</Day>
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<Issue>12</Issue>
<PubDate><Year>1993</Year>
<Month>Apr</Month>
<Day>25</Day>
</PubDate>
</JournalIssue>
<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J Biol Chem</ISOAbbreviation>
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<ArticleTitle>Iodide as the mediator for the reductive reactions of peroxidases.</ArticleTitle>
<Pagination><MedlinePgn>8503-6</MedlinePgn>
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<Abstract><AbstractText>Lignin peroxidase H2 (LiPH2) from the white rot fungus Phanerochaete chrysosporium catalyzed the reduction of cytochrome c, nitro blue tetrazolium, ferric iron, molecular oxygen, and triiodide in a reaction mixture containing LiPH2, H2O2, EDTA, and iodide. Activity followed first order kinetics with respect to EDTA concentration. The reductive activity observed with LiPH2 using iodide as the mediator was comparable to that obtained using a variety of other free radical mediators such as veratryl alcohol, 1,4-dimethoxybenzene, and 1,2,3- and 1,2,4-trimethoxybenzene. EDTA-derived radicals were detected by ESR spin trapping upon incubation of LiPH2 with H2O2, iodide, and EDTA. Reduction activity was also observed using other peroxidases such as lactoperoxidase, horseradish peroxidase, and myeloperoxidase. For the reduction activity of LiPH2, it is proposed that the oxidation of EDTA is mediated by the iodide radical, and the reduction of various electron acceptors is mediated by EDTA radicals. The inhibition of reduction activity at higher concentrations of iodide might be due to the combination of iodide radicals to form I2 which forms a stable triiodide complex by reacting with excess iodide.</AbstractText>
</Abstract>
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<Language>eng</Language>
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<MeshHeading><DescriptorName UI="D004492" MajorTopicYN="N">Edetic Acid</DescriptorName>
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<MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName>
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<MeshHeading><DescriptorName UI="D009195" MajorTopicYN="N">Peroxidase</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
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Iodide as the mediator for the reductive reactions of peroxidases.

Iodide as the mediator for the reductive reactions of peroxidases.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki