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Carbon Monoxide Dehydrogenase Reduces Cyanate to Cyanide
Author(s) -
Ciaccafava Alexandre,
Tombolelli Daria,
Domnik Lilith,
Jeoung JaeHun,
Dobbek Holger,
Mroginski MariaAndrea,
Zebger Ingo,
Hildebrandt Peter
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201703225
Subject(s) - carbon monoxide dehydrogenase , cyanate , chemistry , cyanide , adduct , carbon monoxide , catalysis , potassium cyanide , catalytic cycle , enzyme , stereochemistry , combinatorial chemistry , organic chemistry
Abstract The biocatalytic function of carbon monoxide dehydrogenase (CODH) has a high environmental relevance owing to its ability to reduce CO 2 . 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 − ) to cyanide (CN − ) reduction at the C‐cluster. The adduct remains bound to the catalytic center to form the so‐called CN − ‐inhibited state. Notably, this conversion does not occur in crystals of the Carboxydothermus hydrogenoformans CODH enzyme (CODHII Ch ), as indicated by the lack of the corresponding CN − stretching mode. The transformation of NCO − , which also acts as an inhibitor of the two‐electron‐reduced C red2 state of CODH, could thus mimic CO 2 turnover and open new perspectives for elucidation of the detailed catalytic mechanism of CODH.