Small Molecules Govern Thiol Redox Switches.
Identifieur interne : 000215 ( Main/Exploration ); précédent : 000214; suivant : 000216Small Molecules Govern Thiol Redox Switches.
Auteurs : Johannes Knuesting [Allemagne] ; Renate Scheibe [Allemagne]Source :
- Trends in plant science [ 1878-4372 ] ; 2018.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Chloroplastes, Oxygène, Thiols.
- Oxydoréduction, Photosynthèse, Stress oxydatif, Transduction du signal.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Oxygen, Sulfhydryl Compounds.
- metabolism : Chloroplasts.
- Oxidation-Reduction, Oxidative Stress, Photosynthesis, Signal Transduction.
Abstract
Oxygenic photosynthesis gave rise to a regulatory mechanism based on reversible redox-modifications of enzymes. In chloroplasts, such on-off switches separate metabolic pathways to avoid futile cycles. During illumination, the redox interconversions allow for rapidly and finely adjusting activation states of redox-regulated enzymes. Noncovalent effects by metabolites binding to these enzymes, here addressed as 'small molecules', affect the rates of reduction and oxidation. The chloroplast enzymes provide an example for a versatile regulatory principle where small molecules govern thiol switches to integrate redox state and metabolism for an appropriate response to environmental challenges. In general, this principle can be transferred to reactive thiols involved in redox signaling, oxidative stress responses, and in disease of all organisms.
DOI: 10.1016/j.tplants.2018.06.007
PubMed: 30149854
Affiliations:
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In chloroplasts, such on-off switches separate metabolic pathways to avoid futile cycles. During illumination, the redox interconversions allow for rapidly and finely adjusting activation states of redox-regulated enzymes. Noncovalent effects by metabolites binding to these enzymes, here addressed as 'small molecules', affect the rates of reduction and oxidation. The chloroplast enzymes provide an example for a versatile regulatory principle where small molecules govern thiol switches to integrate redox state and metabolism for an appropriate response to environmental challenges. In general, this principle can be transferred to reactive thiols involved in redox signaling, oxidative stress responses, and in disease of all organisms.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30149854</PMID><DateCompleted><Year>2019</Year><Month>04</Month><Day>09</Day></DateCompleted><DateRevised><Year>2019</Year><Month>04</Month><Day>09</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1878-4372</ISSN><JournalIssue CitedMedium="Internet"><Volume>23</Volume><Issue>9</Issue><PubDate><Year>2018</Year><Month>09</Month></PubDate></JournalIssue><Title>Trends in plant science</Title><ISOAbbreviation>Trends Plant Sci</ISOAbbreviation></Journal><ArticleTitle>Small Molecules Govern Thiol Redox Switches.</ArticleTitle><Pagination><MedlinePgn>769-782</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S1360-1385(18)30137-7</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.tplants.2018.06.007</ELocationID><Abstract><AbstractText>Oxygenic photosynthesis gave rise to a regulatory mechanism based on reversible redox-modifications of enzymes. In chloroplasts, such on-off switches separate metabolic pathways to avoid futile cycles. During illumination, the redox interconversions allow for rapidly and finely adjusting activation states of redox-regulated enzymes. Noncovalent effects by metabolites binding to these enzymes, here addressed as 'small molecules', affect the rates of reduction and oxidation. The chloroplast enzymes provide an example for a versatile regulatory principle where small molecules govern thiol switches to integrate redox state and metabolism for an appropriate response to environmental challenges. In general, this principle can be transferred to reactive thiols involved in redox signaling, oxidative stress responses, and in disease of all organisms.</AbstractText><CopyrightInformation>Copyright © 2018 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Knuesting</LastName><ForeName>Johannes</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Plant Physiology, Faculty of Biology and Chemistry, Osnabrück University, Barbarastr. 11, 49076 Osnabrück, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Scheibe</LastName><ForeName>Renate</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Plant Physiology, Faculty of Biology and Chemistry, Osnabrück University, Barbarastr. 11, 49076 Osnabrück, Germany. 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