Small Molecules Govern Thiol Redox Switches

Autor(en): Knuesting, Johannes
Scheibe, Renate 
Stichwörter: CHLOROPLAST ATP SYNTHASE; DEPENDENT REGULATION; DISULFIDE EXCHANGE; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; LIGHT ACTIVATION; NADP-MALATE DEHYDROGENASE; PHOTOSYNTHETIC ELECTRON-TRANSPORT; Plant Sciences; PLASTIDIAL THIOREDOXINS; STARCH SYNTHESIS; THIOREDOXIN REDUCTASE
Erscheinungsdatum: 2018
Herausgeber: ELSEVIER SCIENCE LONDON
Journal: TRENDS IN PLANT SCIENCE
Volumen: 23
Ausgabe: 9
Startseite: 769
Seitenende: 782
Zusammenfassung: 
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.
ISSN: 13601385
DOI: 10.1016/j.tplants.2018.06.007

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