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JXB Advance Access published online on January 6, 2009
Journal of Experimental Botany, doi:10.1093/jxb/ern309
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© The Author [2009]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

REVIEW-ARTICLE

Occurrence, phylogeny, structure, and function of catalases and peroxidases in cyanobacteria

Margit Bernroitner1, Marcel Zamocky1,2, Paul G. Furtmüller1, Günter A. Peschek3 and Christian Obinger1,*

1BOKU–University of Natural Resources and Applied Life Sciences, Department of Chemistry, Metalloprotein Research Group, A-1190 Vienna, Austria
2Institute of Molecular Biology, Slovak Academy of Sciences, Dubravska cesta 21, SK-84251 Bratislava, Slovakia
3Institute of Physical Chemistry, Molecular Bioenergetics Group, University of Vienna, Althanstraße 14, A-1090 Vienna, Austria

* To whom correspondence should be addressed. E-mail: christian.obinger{at}boku.ac.at

Cyanobacteria have evolved ~3x109 years ago from ancient phototrophic microorganisms that already lived on our planet Earth. By opening the era of an aerobic, oxygen-containing biosphere, they are the true pacemakers of geological and biological evolution. Cyanobacteria must have been among the first organisms to elaborate mechanisms for the detoxification of partially reduced oxygen species including (hydrogen) peroxide. Since there is still an suprising lack of knowledge on the type, role, and mechanism(s) of peroxide-degrading enzymes in these bacteria, all 44 fully or partially sequenced genomes for haem and non-haem catalases and peroxidases have been critically analysed based on well known structure–function relationships of the corresponding oxidoreductases. It is demonstrated that H2O2-dismutating enzymes are mainly represented by bifunctional (haem) catalase–peroxidases and (binuclear) manganese catalases, with the latter being almost exclusively found in diazotrophic species. Several strains even lack a gene that encodes an enzyme with catalase activity. Two groups of peroxidases are found. Genes encoding putative (primordial) haem peroxidases (with homology to corresponding mammalian enzymes) and vanadium-containing iodoperoxidases are found only in a few species, whereas genes encoding peroxiredoxins (1-Cys, 2-Cys, type II, and Q-type) are ubiquitous in cyanobacteria. In addition, ~70% contain NADPH-dependent glutathione peroxidase-like proteins. The occurrence and phylogeny of these enzymes is discussed, as well as the present knowledge of their physiological role(s).

Key words: Catalase–peroxidase, Cyanobacterium, glutathione peroxidase, manganese catalase, oxidative stress, peroxide detoxification, peroxiredoxin, vanadium peroxidase

Received 17 September 2008; Accepted 10 November 2008


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