Significance of plant sulfite oxidase.
Identifieur interne : 003A76 ( Main/Exploration ); précédent : 003A75; suivant : 003A77Significance of plant sulfite oxidase.
Auteurs : R. H Nsch [Allemagne] ; C. Lang ; H. Rennenberg ; R R MendelSource :
- Plant biology (Stuttgart, Germany) [ 1435-8603 ] ; 2007.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Plantes.
- métabolisme : Molybdène, Soufre, Sulfite oxidase.
- Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Molybdenum, Sulfite Oxidase, Sulfur.
- enzymology : Plants.
- Oxidation-Reduction.
Abstract
Sulfite oxidizing activities are known since years in animals, microorganisms, and also plants. Among plants, the only enzyme well characterized on molecular and biochemical level is the molybdoenzyme sulfite oxidase (SO). It oxidizes sulfite using molecular oxygen as electron acceptor, leading to the production of sulfate and hydrogen peroxide. The latter reaction product seems to be the reason why plant SO is localized in peroxisomes, because peroxisomal catalase is able to decompose hydrogen peroxide. On the other hand, we have indications for an additional reaction taking place in peroxisomes: sulfite can be nonenzymatically oxidized by hydrogen peroxide. This will promote the detoxification of hydrogen peroxide especially in the case of high amounts of sulfite. Hence we assume that SO could possibly serve as "safety valve" for detoxifying excess amounts of sulfite and protecting the cell from sulfitolysis. Supportive evidence for this assumption comes from experiments where we fumigated transgenic poplar plants overexpressing ARABIDOPSIS SO with SO(2) gas. In this paper, we try to explain sulfite oxidation in its co-regulation with sulfate assimilation and summarize other sulfite oxidizing activities described in plants. Finally we discuss the importance of sulfite detoxification in plants.
DOI: 10.1055/s-2007-965433
PubMed: 17853359
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Rennenberg</name></author><author><name sortKey="Mendel, R R" sort="Mendel, R R" uniqKey="Mendel R" first="R R" last="Mendel">R R Mendel</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17853359</idno><idno type="pmid">17853359</idno><idno type="doi">10.1055/s-2007-965433</idno><idno type="wicri:Area/Main/Corpus">003A76</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">003A76</idno><idno type="wicri:Area/Main/Curation">003A76</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">003A76</idno><idno type="wicri:Area/Main/Exploration">003A76</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Significance of plant sulfite oxidase.</title><author><name sortKey="H Nsch, R" sort="H Nsch, R" uniqKey="H Nsch R" first="R" last="H Nsch">R. H Nsch</name><affiliation wicri:level="1"><nlm:affiliation>Department of Plant Biology, Technical University of Braunschweig, Humboldtstrasse 1, 38106 Braunschweig, Germany. r.haensch@tu-bs.de</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Plant Biology, Technical University of Braunschweig, Humboldtstrasse 1, 38106 Braunschweig</wicri:regionArea><wicri:noRegion>38106 Braunschweig</wicri:noRegion><wicri:noRegion>38106 Braunschweig</wicri:noRegion><wicri:noRegion>38106 Braunschweig</wicri:noRegion></affiliation></author><author><name sortKey="Lang, C" sort="Lang, C" uniqKey="Lang C" first="C" last="Lang">C. Lang</name></author><author><name sortKey="Rennenberg, H" sort="Rennenberg, H" uniqKey="Rennenberg H" first="H" last="Rennenberg">H. Rennenberg</name></author><author><name sortKey="Mendel, R R" sort="Mendel, R R" uniqKey="Mendel R" first="R R" last="Mendel">R R Mendel</name></author></analytic><series><title level="j">Plant biology (Stuttgart, Germany)</title><idno type="ISSN">1435-8603</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Molybdenum (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Plants (enzymology)</term><term>Sulfite Oxidase (metabolism)</term><term>Sulfur (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Molybdène (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Plantes (enzymologie)</term><term>Soufre (métabolisme)</term><term>Sulfite oxidase (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Molybdenum</term><term>Sulfite Oxidase</term><term>Sulfur</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Plantes</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Plants</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Molybdène</term><term>Soufre</term><term>Sulfite oxidase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Sulfite oxidizing activities are known since years in animals, microorganisms, and also plants. Among plants, the only enzyme well characterized on molecular and biochemical level is the molybdoenzyme sulfite oxidase (SO). It oxidizes sulfite using molecular oxygen as electron acceptor, leading to the production of sulfate and hydrogen peroxide. The latter reaction product seems to be the reason why plant SO is localized in peroxisomes, because peroxisomal catalase is able to decompose hydrogen peroxide. On the other hand, we have indications for an additional reaction taking place in peroxisomes: sulfite can be nonenzymatically oxidized by hydrogen peroxide. This will promote the detoxification of hydrogen peroxide especially in the case of high amounts of sulfite. Hence we assume that SO could possibly serve as "safety valve" for detoxifying excess amounts of sulfite and protecting the cell from sulfitolysis. Supportive evidence for this assumption comes from experiments where we fumigated transgenic poplar plants overexpressing ARABIDOPSIS SO with SO(2) gas. In this paper, we try to explain sulfite oxidation in its co-regulation with sulfate assimilation and summarize other sulfite oxidizing activities described in plants. Finally we discuss the importance of sulfite detoxification in plants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17853359</PMID><DateCompleted><Year>2007</Year><Month>11</Month><Day>13</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1435-8603</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><Issue>5</Issue><PubDate><Year>2007</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Plant biology (Stuttgart, Germany)</Title><ISOAbbreviation>Plant Biol (Stuttg)</ISOAbbreviation></Journal><ArticleTitle>Significance of plant sulfite oxidase.</ArticleTitle><Pagination><MedlinePgn>589-95</MedlinePgn></Pagination><Abstract><AbstractText>Sulfite oxidizing activities are known since years in animals, microorganisms, and also plants. Among plants, the only enzyme well characterized on molecular and biochemical level is the molybdoenzyme sulfite oxidase (SO). It oxidizes sulfite using molecular oxygen as electron acceptor, leading to the production of sulfate and hydrogen peroxide. The latter reaction product seems to be the reason why plant SO is localized in peroxisomes, because peroxisomal catalase is able to decompose hydrogen peroxide. On the other hand, we have indications for an additional reaction taking place in peroxisomes: sulfite can be nonenzymatically oxidized by hydrogen peroxide. This will promote the detoxification of hydrogen peroxide especially in the case of high amounts of sulfite. Hence we assume that SO could possibly serve as "safety valve" for detoxifying excess amounts of sulfite and protecting the cell from sulfitolysis. Supportive evidence for this assumption comes from experiments where we fumigated transgenic poplar plants overexpressing ARABIDOPSIS SO with SO(2) gas. In this paper, we try to explain sulfite oxidation in its co-regulation with sulfate assimilation and summarize other sulfite oxidizing activities described in plants. Finally we discuss the importance of sulfite detoxification in plants.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hänsch</LastName><ForeName>R</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Plant Biology, Technical University of Braunschweig, Humboldtstrasse 1, 38106 Braunschweig, Germany. r.haensch@tu-bs.de</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lang</LastName><ForeName>C</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Rennenberg</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Mendel</LastName><ForeName>R R</ForeName><Initials>RR</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Plant Biol (Stuttg)</MedlineTA><NlmUniqueID>101148926</NlmUniqueID><ISSNLinking>1435-8603</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>70FD1KFU70</RegistryNumber><NameOfSubstance UI="D013455">Sulfur</NameOfSubstance></Chemical><Chemical><RegistryNumber>81AH48963U</RegistryNumber><NameOfSubstance UI="D008982">Molybdenum</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.3.1</RegistryNumber><NameOfSubstance UI="D050876">Sulfite Oxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D008982" MajorTopicYN="N">Molybdenum</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050876" MajorTopicYN="N">Sulfite Oxidase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013455" MajorTopicYN="N">Sulfur</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>49</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>9</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>11</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>9</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17853359</ArticleId><ArticleId IdType="doi">10.1055/s-2007-965433</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Lang, C" sort="Lang, C" uniqKey="Lang C" first="C" last="Lang">C. Lang</name><name sortKey="Mendel, R R" sort="Mendel, R R" uniqKey="Mendel R" first="R R" last="Mendel">R R Mendel</name><name sortKey="Rennenberg, H" sort="Rennenberg, H" uniqKey="Rennenberg H" first="H" last="Rennenberg">H. Rennenberg</name></noCountry><country name="Allemagne"><noRegion><name sortKey="H Nsch, R" sort="H Nsch, R" uniqKey="H Nsch R" first="R" last="H Nsch">R. H Nsch</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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