{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T03:19:10Z","timestamp":1791343150816,"version":"4.3.1"},"reference-count":31,"publisher":"Wiley","issue":"14","license":[{"start":{"date-parts":[[2013,9,3]],"date-time":"2013-09-03T00:00:00Z","timestamp":1378166400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["chemistry-europe.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["ChemBioChem"],"published-print":{"date-parts":[[2013,9,23]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Carbon monoxide dehydrogenases (CODHs) catalyse the reversible conversion between CO and CO<jats:sub>2<\/jats:sub>. Several small molecules or ions are inhibitors and probes for different oxidation states of the unusual [Ni\u20104\u2009Fe\u20104\u2009S] cluster that forms the active site. The actions of these small probes on two enzymes\u2014CODH I<jats:sub><jats:italic>Ch<\/jats:italic><\/jats:sub> and CODH II<jats:sub><jats:italic>Ch<\/jats:italic><\/jats:sub>\u2014produced by <jats:italic>Carboxydothermus hydrogenoformans<\/jats:italic> have been studied by protein film voltammetry to compare their behaviour and to establish general characteristics. Whereas CODH I<jats:sub><jats:italic>Ch<\/jats:italic><\/jats:sub> is, so far, the better studied of the two isozymes in terms of its electrocatalytic properties, it is CODH II<jats:sub><jats:italic>Ch<\/jats:italic><\/jats:sub> that has been characterised by X\u2010ray crystallography. The two isozymes, which share 58.3\u2009% sequence identity and 73.9\u2009% sequence similarity, show similar patterns of behaviour with regard to selective inhibition of CO<jats:sub>2<\/jats:sub> reduction by CO (product) and cyanate, potent and selective inhibition of CO oxidation by cyanide, and the action of sulfide, which promotes oxidative inactivation of the enzyme. For both isozymes, rates of binding of substrate analogues CN<jats:sup>\u2212<\/jats:sup> (for CO) and NCO<jats:sup>\u2212<\/jats:sup> (for CO<jats:sub>2<\/jats:sub>) are orders of magnitude lower than turnover, a feature that is clearly revealed through hysteresis of cyclic voltammetry. Inhibition by CN<jats:sup>\u2212<\/jats:sup> and CO is much stronger for CODH II<jats:sub><jats:italic>Ch<\/jats:italic><\/jats:sub> than for CODH I<jats:sub><jats:italic>Ch,<\/jats:italic><\/jats:sub> a property that has relevance for applying these enzymes as model catalysts in solar\u2010driven CO<jats:sub>2<\/jats:sub> reduction.<\/jats:p>","DOI":"10.1002\/cbic.201300270","type":"journal-article","created":{"date-parts":[[2013,9,3]],"date-time":"2013-09-03T09:17:55Z","timestamp":1378199875000},"page":"1845-1851","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":50,"title":["Investigations of Two Bidirectional Carbon Monoxide Dehydrogenases from <i>Carboxydothermus hydrogenoformans<\/i> by Protein Film Electrochemistry"],"prefix":"10.1002","volume":"14","author":[{"given":"Vincent C.\u2010C.","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephen 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