Plant peroxiredoxins

Dietz K-J (2003)

No fulltext has been uploaded. References only!
Journal Article | Review | Published | English

No fulltext has been uploaded

Abstract / Notes
Peroxiredoxins (Prxs) are abundant low-efficiency peroxidases located in distinct cell compartments including the chloroplast and mitochondrion. They are grouped into four clans based on their structural and biochemical properties. The catalytic center contains a cysteinyl residue that reduces diverse peroxides and is regenerated via intramolecular or intermolecular thiol-disulfide-reactions and finally by electron donors such as thioredoxins and glutaredoxins. Prxs show a complex regulation by endogenous and environmental stimuli at both the transcript and protein levels. In addition to their role in antioxidant defense in photosynthesis, respiration, and stress response, they may also be involved in modulating redox signaling during development and adaptation.
Publishing Year

Cite this

Dietz K-J. Plant peroxiredoxins. ANNUAL REVIEW OF PLANT BIOLOGY. 2003;54:93-107.
Dietz, K. - J. (2003). Plant peroxiredoxins. ANNUAL REVIEW OF PLANT BIOLOGY, 54, 93-107. doi:10.1146/ammurev.arplant.54.031902.134934
Dietz, K. - J. (2003). Plant peroxiredoxins. ANNUAL REVIEW OF PLANT BIOLOGY 54, 93-107.
Dietz, K.-J., 2003. Plant peroxiredoxins. ANNUAL REVIEW OF PLANT BIOLOGY, 54, p 93-107.
K.-J. Dietz, “Plant peroxiredoxins”, ANNUAL REVIEW OF PLANT BIOLOGY, vol. 54, 2003, pp. 93-107.
Dietz, K.-J.: Plant peroxiredoxins. ANNUAL REVIEW OF PLANT BIOLOGY. 54, 93-107 (2003).
Dietz, Karl-Josef. “Plant peroxiredoxins”. ANNUAL REVIEW OF PLANT BIOLOGY 54 (2003): 93-107.
This data publication is cited in the following publications:
This publication cites the following data publications:

185 Citations in Europe PMC

Data provided by Europe PubMed Central.

Redox regulation: a broadening horizon.
Buchanan BB, Balmer Y., Annu Rev Plant Biol 56(), 2005
PMID: 15862094
Making the life of heavy metal-stressed plants a little easier.
Gratao PL, Polle A, Lea PJ, Azevedo RA., Functional plant biology : FPB. 32(6), 2005
PMID: IND43727070
The thioredoxin h system of higher plants.
Gelhaye E, Rouhier N, Jacquot JP., Plant Physiol Biochem 42(4), 2004
PMID: 15120110
New thioredoxin targets in the unicellular photosynthetic eukaryote Chlamydomonas reinhardtii.
Lemaire SD, Guillon B, Le Maréchal P, Keryer E, Miginiac-Maslow M, Decottignies P., Proc Natl Acad Sci U S A 101(19), 2004
PMID: 15123830
Cadmium toxicity to barley (Hordeum vulgare) as affected by varying Fe nutritional status.
Sharma SS, Kaul S, Metwally A, Goyal KC, Finkemeier I, Dietz KJ., Plant Sci 166(5), 2004
PMID: IND43633715
Specific changes in the Arabidopsis proteome in response to bacterial challenge: differentiating basal and R-gene mediated resistance.
Jones AM, Thomas V, Truman B, Lilley K, Mansfield J, Grant M., Phytochemistry 65(12), 2004
PMID: 15276439
Molecular characterization of peroxiredoxin from Entamoeba moshkovskii and a comparison with Entamoeba histolytica.
Cheng XJ, Yoshihara E, Takeuchi T, Tachibana H., Mol Biochem Parasitol 138(2), 2004
PMID: 15555731

57 References

Data provided by Europe PubMed Central.

Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution.
Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE., Nat. Struct. Biol. 5(5), 1998
PMID: 9587003
Hofmann B, Hecht HJ, Flohe L., Biol. Chem. 383(3-4), 2002
PMID: 12033427
Induction of an antioxidant protein of Saccharomyces cerevisiae by O2, Fe3+, or 2-mercaptoethanol.
Kim IH, Kim K, Rhee SG., Proc. Natl. Acad. Sci. U.S.A. 86(16), 1989
PMID: 2668950
Dimerization of thiol-specific antioxidant and the essential role of cysteine 47.
Chae HZ, Uhm TB, Rhee SG., Proc. Natl. Acad. Sci. U.S.A. 91(15), 1994
PMID: 8041739


0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®


PMID: 14502986
PubMed | Europe PMC

Search this title in

Google Scholar