Oxidation of halides by peroxidases and their subsequent reductions.
Identifieur interne : 000E33 ( Main/Curation ); précédent : 000E32; suivant : 000E34Oxidation of halides by peroxidases and their subsequent reductions.
Auteurs : M M Shah ; S D AustSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 1993.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Agaricales.
- métabolisme : Iodide peroxidase, Iodures, Peroxidases.
- pharmacologie : Acide édétique, Iodures.
- Cinétique, Modèles théoriques, Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Iodide Peroxidase, Iodides, Peroxidases.
- chemical , pharmacology : Edetic Acid, Iodides.
- enzymology : Agaricales.
- Kinetics, Models, Theoretical, Oxidation-Reduction.
Abstract
The iodide oxidase activity and iodide-dependent pseudocatalatic activity of lignin peroxidase H2, an extracellular enzyme of the white rot fungus Phanerochaete chrysosporium, was inhibited by EDTA. The inhibition of iodide oxidase activity by EDTA was reversed at higher concentrations of iodide. Similar results were observed with a number of peroxidases. On further investigation, it was found that EDTA was decarboxylated in a reaction mixture containing a peroxidase, iodide, H2O2, and EDTA. EDTA was also decarboxylated by hypoiodite, a possible intermediate during oxidation of iodide by peroxidases. Iodide-dependent pseudocatalatic activity was increased with an increase in the concentration of H2O2 and inhibited at higher concentrations of iodide. EDTA was also oxidized by horseradish peroxidase, lactoperoxidase, and myeloperoxidase using iodide or bromide as a mediator. However, only myeloperoxidase was able to decarboxylate EDTA using chloride as a mediator. It is proposed that halide is oxidized to hypohalite by peroxidases. The hypohalite is then reduced by EDTA, H2O2, or halide. Reduction is associated with the decarboxylation of EDTA, oxidation of H2O2 to molecular oxygen, or oxidation of halide.
DOI: 10.1006/abbi.1993.1035
PubMed: 8424660
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M M Shah<affiliation><nlm:affiliation>Biotechnology Center, Utah State University, Logan 84322-4705.</nlm:affiliation><wicri:noCountry code="subField">Logan 84322-4705</wicri:noCountry></affiliation>Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Oxidation of halides by peroxidases and their subsequent reductions.</title><author><name sortKey="Shah, M M" sort="Shah, M M" uniqKey="Shah M" first="M M" last="Shah">M M Shah</name><affiliation><nlm:affiliation>Biotechnology Center, Utah State University, Logan 84322-4705.</nlm:affiliation><wicri:noCountry code="subField">Logan 84322-4705</wicri:noCountry></affiliation></author><author><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1993">1993</date><idno type="RBID">pubmed:8424660</idno><idno type="pmid">8424660</idno><idno type="doi">10.1006/abbi.1993.1035</idno><idno type="wicri:Area/Main/Corpus">000E33</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000E33</idno><idno type="wicri:Area/Main/Curation">000E33</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000E33</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Oxidation of halides by peroxidases and their subsequent reductions.</title><author><name sortKey="Shah, M M" sort="Shah, M M" uniqKey="Shah M" first="M M" last="Shah">M M Shah</name><affiliation><nlm:affiliation>Biotechnology Center, Utah State University, Logan 84322-4705.</nlm:affiliation><wicri:noCountry code="subField">Logan 84322-4705</wicri:noCountry></affiliation></author><author><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name></author></analytic><series><title level="j">Archives of biochemistry and biophysics</title><idno type="ISSN">0003-9861</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Agaricales (enzymology)</term><term>Edetic Acid (pharmacology)</term><term>Iodide Peroxidase (metabolism)</term><term>Iodides (metabolism)</term><term>Iodides (pharmacology)</term><term>Kinetics (MeSH)</term><term>Models, Theoretical (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide édétique (pharmacologie)</term><term>Agaricales (enzymologie)</term><term>Cinétique (MeSH)</term><term>Iodide peroxidase (métabolisme)</term><term>Iodures (métabolisme)</term><term>Iodures (pharmacologie)</term><term>Modèles théoriques (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Iodide Peroxidase</term><term>Iodides</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Edetic Acid</term><term>Iodides</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Iodide peroxidase</term><term>Iodures</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acide édétique</term><term>Iodures</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Kinetics</term><term>Models, Theoretical</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Modèles théoriques</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The iodide oxidase activity and iodide-dependent pseudocatalatic activity of lignin peroxidase H2, an extracellular enzyme of the white rot fungus Phanerochaete chrysosporium, was inhibited by EDTA. The inhibition of iodide oxidase activity by EDTA was reversed at higher concentrations of iodide. Similar results were observed with a number of peroxidases. On further investigation, it was found that EDTA was decarboxylated in a reaction mixture containing a peroxidase, iodide, H2O2, and EDTA. EDTA was also decarboxylated by hypoiodite, a possible intermediate during oxidation of iodide by peroxidases. Iodide-dependent pseudocatalatic activity was increased with an increase in the concentration of H2O2 and inhibited at higher concentrations of iodide. EDTA was also oxidized by horseradish peroxidase, lactoperoxidase, and myeloperoxidase using iodide or bromide as a mediator. However, only myeloperoxidase was able to decarboxylate EDTA using chloride as a mediator. It is proposed that halide is oxidized to hypohalite by peroxidases. The hypohalite is then reduced by EDTA, H2O2, or halide. Reduction is associated with the decarboxylation of EDTA, oxidation of H2O2 to molecular oxygen, or oxidation of halide.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8424660</PMID><DateCompleted><Year>1993</Year><Month>02</Month><Day>23</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-9861</ISSN><JournalIssue CitedMedium="Print"><Volume>300</Volume><Issue>1</Issue><PubDate><Year>1993</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Oxidation of halides by peroxidases and their subsequent reductions.</ArticleTitle><Pagination><MedlinePgn>253-7</MedlinePgn></Pagination><Abstract><AbstractText>The iodide oxidase activity and iodide-dependent pseudocatalatic activity of lignin peroxidase H2, an extracellular enzyme of the white rot fungus Phanerochaete chrysosporium, was inhibited by EDTA. The inhibition of iodide oxidase activity by EDTA was reversed at higher concentrations of iodide. Similar results were observed with a number of peroxidases. On further investigation, it was found that EDTA was decarboxylated in a reaction mixture containing a peroxidase, iodide, H2O2, and EDTA. EDTA was also decarboxylated by hypoiodite, a possible intermediate during oxidation of iodide by peroxidases. Iodide-dependent pseudocatalatic activity was increased with an increase in the concentration of H2O2 and inhibited at higher concentrations of iodide. EDTA was also oxidized by horseradish peroxidase, lactoperoxidase, and myeloperoxidase using iodide or bromide as a mediator. However, only myeloperoxidase was able to decarboxylate EDTA using chloride as a mediator. It is proposed that halide is oxidized to hypohalite by peroxidases. The hypohalite is then reduced by EDTA, H2O2, or halide. Reduction is associated with the decarboxylation of EDTA, oxidation of H2O2 to molecular oxygen, or oxidation of halide.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shah</LastName><ForeName>M M</ForeName><Initials>MM</Initials><AffiliationInfo><Affiliation>Biotechnology Center, Utah State University, Logan 84322-4705.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aust</LastName><ForeName>S D</ForeName><Initials>SD</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>ES04922</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Arch Biochem Biophys</MedlineTA><NlmUniqueID>0372430</NlmUniqueID><ISSNLinking>0003-9861</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007454">Iodides</NameOfSubstance></Chemical><Chemical><RegistryNumber>9G34HU7RV0</RegistryNumber><NameOfSubstance UI="D004492">Edetic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.8</RegistryNumber><NameOfSubstance UI="D007453">Iodide Peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000363" MajorTopicYN="N">Agaricales</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004492" MajorTopicYN="N">Edetic Acid</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007453" MajorTopicYN="N">Iodide Peroxidase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007454" MajorTopicYN="N">Iodides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008962" MajorTopicYN="N">Models, Theoretical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1993</Year><Month>1</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1993</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1993</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8424660</ArticleId><ArticleId IdType="pii">S0003-9861(83)71035-0</ArticleId><ArticleId IdType="doi">10.1006/abbi.1993.1035</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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