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Beside the water\u2010splitting manganese complex of photosystem <jats:styled-content style=\"fixed-case\">II<\/jats:styled-content>, this metalloenzyme is the second known enzyme that catalyses the formation of a covalent oxygen\u2013oxygen bond. All cyanobacterial <jats:styled-content style=\"fixed-case\">C<\/jats:styled-content>lds have a truncated <jats:styled-content style=\"fixed-case\">N<\/jats:styled-content>\u2010terminus and are dimeric (i.e. clade 2) proteins. As model protein, <jats:styled-content style=\"fixed-case\">C<\/jats:styled-content>ld from <jats:styled-content style=\"fixed-case\"><jats:italic>C<\/jats:italic><\/jats:styled-content><jats:italic>yanothece<\/jats:italic> sp. <jats:styled-content style=\"fixed-case\">PCC<\/jats:styled-content>7425 (<jats:styled-content style=\"fixed-case\">CC<\/jats:styled-content>ld) was recombinantly produced in <jats:styled-content style=\"fixed-case\"><jats:italic>E<\/jats:italic><\/jats:styled-content><jats:italic>scherichia\u2009coli<\/jats:italic> and shown to efficiently degrade chlorite with an activity optimum at <jats:styled-content style=\"fixed-case\">pH<\/jats:styled-content> 5.0 [<jats:italic>k<\/jats:italic><jats:sub>cat<\/jats:sub> 1144\u2009\u00b1\u200923.8\u2009s<jats:sup>\u22121<\/jats:sup>, <jats:styled-content style=\"fixed-case\"><jats:italic>K<\/jats:italic><jats:sub>M<\/jats:sub><\/jats:styled-content> 162\u2009\u00b1\u200910.0\u2009\u03bcM, catalytic efficiency (7.1\u2009\u00b1\u20090.6)\u2009\u00d7\u200910<jats:sup>6<\/jats:sup>\u2009M<jats:sup>\u22121<\/jats:sup>\u2009s<jats:sup>\u22121<\/jats:sup>]. The resting ferric high\u2010spin axially symmetric heme enzyme has a standard reduction potential of the <jats:styled-content style=\"fixed-case\">F<\/jats:styled-content>e(<jats:styled-content style=\"fixed-case\">III<\/jats:styled-content>)\/<jats:styled-content style=\"fixed-case\">F<\/jats:styled-content>e(<jats:styled-content style=\"fixed-case\">II<\/jats:styled-content>) couple of \u2212126\u2009\u00b1\u20091.9\u2009mV at <jats:styled-content style=\"fixed-case\">pH<\/jats:styled-content> 7.0. Cyanide mediates the formation of a low\u2010spin complex with <jats:italic>k<\/jats:italic><jats:sub>on<\/jats:sub>\u2009=\u2009(1.6\u2009\u00b1\u20090.1)\u2009\u00d7\u200910<jats:sup>5<\/jats:sup>\u2009M<jats:sup>\u22121<\/jats:sup>\u2009s<jats:sup>\u22121<\/jats:sup> and <jats:italic>k<\/jats:italic><jats:sub>off<\/jats:sub>\u2009=\u20091.4\u2009\u00b1\u20092.9\u2009s<jats:sup>\u22121<\/jats:sup> (<jats:styled-content style=\"fixed-case\"><jats:italic>K<\/jats:italic><jats:sub>D<\/jats:sub><\/jats:styled-content>\u2009\u223c\u20098.6\u2009\u03bcM). Both, thermal and chemical unfolding follows a non\u2010two\u2010state unfolding pathway with the first transition being related to the release of the prosthetic group. The obtained data are discussed with respect to known structure\u2013function relationships of <jats:styled-content style=\"fixed-case\">C<\/jats:styled-content>lds. We ask for the physiological substrate and putative function of these <jats:styled-content style=\"fixed-case\">O<jats:sub>2<\/jats:sub><\/jats:styled-content>\u2010producing proteins in (nitrogen\u2010fixing) cyanobacteria.<\/jats:p>","DOI":"10.1111\/mmi.12989","type":"journal-article","created":{"date-parts":[[2015,3,3]],"date-time":"2015-03-03T06:54:48Z","timestamp":1425365688000},"page":"1053-1068","source":"Crossref","is-referenced-by-count":25,"title":["Dimeric chlorite dismutase from the nitrogen\u2010fixing cyanobacterium <scp><i>C<\/i><\/scp><i>yanothece<\/i> sp. <scp>PCC<\/scp>7425"],"prefix":"10.1111","volume":"96","author":[{"given":"Irene","family":"Schaffner","sequence":"first","affiliation":[{"name":"Department of Chemistry Division of Biochemistry BOKU \u2013 University of Natural Resources and Life Sciences  Muthgasse 18 A\u20101190 Vienna Austria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stefan","family":"Hofbauer","sequence":"additional","affiliation":[{"name":"Department of Chemistry Division of Biochemistry BOKU \u2013 University of Natural Resources and Life Sciences  Muthgasse 18 A\u20101190 Vienna Austria"},{"name":"Department for Structural and Computational Biology Max F. Perutz Laboratories University of Vienna  Vienna Austria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael","family":"Krutzler","sequence":"additional","affiliation":[{"name":"Department of Chemistry Division of Biochemistry BOKU \u2013 University of Natural Resources and Life Sciences  Muthgasse 18 A\u20101190 Vienna Austria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Katharina F.","family":"Pirker","sequence":"additional","affiliation":[{"name":"Department of Chemistry Division of Biochemistry BOKU \u2013 University of Natural Resources and Life Sciences  Muthgasse 18 A\u20101190 Vienna Austria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marzia","family":"Bellei","sequence":"additional","affiliation":[{"name":"Department of Life Sciences University of Modena and Reggio Emilia  41125 Modena Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gerhard","family":"Stadlmayr","sequence":"additional","affiliation":[{"name":"Department of Chemistry Division of Biochemistry BOKU \u2013 University of Natural Resources and Life Sciences  Muthgasse 18 A\u20101190 Vienna Austria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Georg","family":"Mlynek","sequence":"additional","affiliation":[{"name":"Department for Structural and Computational Biology Max F. 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