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Carbon Monoxide Dehydrogenase Reduces Cyanate to Cyanide
Citation key ISI:000403017000007
Author Ciaccafava, Alexandre and Tombolelli, Daria and Domnik, Lilith and Jeoung, Jae-Hun and Dobbek, Holger and Mroginski, Maria-Andrea and Zebger, Ingo and Hildebrandt, Peter
Pages 7398-7401
Year 2017
ISSN 1433-7851
DOI 10.1002/anie.201703225
Address POSTFACH 101161, 69451 WEINHEIM, GERMANY
Journal ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 56
Number 26
Month JUN 19
Publisher WILEY-V C H VERLAG GMBH
Abstract The biocatalytic function of carbon monoxide dehydrogenase (CODH) has a high environmental relevance owing to its ability to reduce CO2. 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 (CODHIICh), 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 CO2 turnover and open new perspectives for elucidation of the detailed catalytic mechanism of CODH.
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