Plant thioredoxins: the multiplicity conundrum

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dc.contributor.authorBaumann, U.
dc.contributor.authorJuttner, J.
dc.contributor.organisationAustralian Centre for Plant Functional Genomics (ACPFG)
dc.date.issued2002
dc.descriptionThe original publication can be found at www.springerlink.com
dc.description.abstractThioredoxins are small proteins distinguished by the presence of a conserved dicysteine active site. In oxidized thioredoxin, the two cysteines form a disulfide bond that is targeted by the enzyme thioredoxin reductase. Together with an electron donor, thioredoxin and thioredoxin reductase form the 'thioredoxin system' that is present in all organisms. Thioredoxins participate in dithiol/disulfide exchange reactions with a large range of cellular substrates. Higher plants possess a very complex thioredoxin profile consisting of at least two different thioredoxin systems that contain distinct, multigenic thioredoxin classes which have different intracellular localizations. In this review we summarise the current state of knowledge regarding the function of plant thioredoxins representing all systems and classes.
dc.identifier.citationCellular and Molecular Life Sciences, 2002; 59(6):1042-1057
dc.identifier.doi10.1007/s00018-002-8485-8
dc.identifier.issn1420-682X
dc.identifier.issn1420-9071
dc.identifier.orcidBaumann, U. [0000-0003-1281-598X]
dc.identifier.urihttp://hdl.handle.net/2440/44160
dc.language.isoen
dc.publisherBirkhauser Verlag Ag
dc.source.urihttps://doi.org/10.1007/s00018-002-8485-8
dc.subjectThioredoxin
dc.subjectchloroplast enzyme
dc.subjectredox regulation
dc.subjectNADPH thioredoxin reductase
dc.subjectferredoxin thioredoxin reductase
dc.subjectmultigene family
dc.subjectdisulfide
dc.subjectseed germination
dc.titlePlant thioredoxins: the multiplicity conundrum
dc.typeJournal article
pubs.publication-statusPublished

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