Please use this identifier to cite or link to this item:
|Scopus||Web of Science®||Altmetric|
|Title:||Plant thioredoxins: the multiplicity conundrum|
|Citation:||Cellular and Molecular Life Sciences, 2002; 59(6):1042-1057|
|Publisher:||Birkhauser Verlag Ag|
|Organisation:||Australian Centre for Plant Functional Genomics (ACPFG)|
|Abstract:||Thioredoxins 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.|
|Keywords:||Thioredoxin; chloroplast enzyme; redox regulation; NADPH thioredoxin reductase; ferredoxin thioredoxin reductase; multigene family; disulfide; seed germination|
|Description:||The original publication can be found at www.springerlink.com|
|Appears in Collections:||Australian Centre for Plant Functional Genomics publications|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.