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Despite numerous studies on CODH over the past decades, its catalytic mechanism is not yet fully understood. In the present combined spectroscopic and theoretical study, we report first evidences for a cyanate (NCO<jats:sup>\u2212<\/jats:sup>) to cyanide (CN<jats:sup>\u2212<\/jats:sup>) reduction at the C\u2010cluster. The adduct remains bound to the catalytic center to form the so\u2010called CN<jats:sup>\u2212<\/jats:sup>\u2010inhibited state. Notably, this conversion does not occur in crystals of the <jats:italic>Carboxydothermus hydrogenoformans<\/jats:italic> CODH enzyme (CODHII<jats:sub><jats:italic>Ch<\/jats:italic><\/jats:sub>), as indicated by the lack of the corresponding CN<jats:sup>\u2212<\/jats:sup> stretching mode. The transformation of NCO<jats:sup>\u2212<\/jats:sup>, which also acts as an inhibitor of the two\u2010electron\u2010reduced C<jats:sub>red2<\/jats:sub> state of CODH, could thus mimic CO<jats:sub>2<\/jats:sub> turnover and open new perspectives for elucidation of the detailed catalytic mechanism of CODH.<\/jats:p>","DOI":"10.1002\/anie.201703225","type":"journal-article","created":{"date-parts":[[2017,5,24]],"date-time":"2017-05-24T00:38:15Z","timestamp":1495586295000},"page":"7398-7401","source":"Crossref","is-referenced-by-count":13,"title":["Carbon Monoxide Dehydrogenase Reduces Cyanate to Cyanide"],"prefix":"10.1002","volume":"56","author":[{"given":"Alexandre","family":"Ciaccafava","sequence":"first","affiliation":[{"name":"Institut f\u00fcr Chemie Technische Universit\u00e4t Berlin  Sekretariat PC 14 10623 Berlin Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daria","family":"Tombolelli","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr 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