CODH‐IV: A High‐Efficiency CO‐Scavenging CO Dehydrogenase with Resistance to O2. Issue 48 (2nd November 2017)

• Record Type: Journal Article
• Authors: Domnik, Lilith; Merrouch, Meriem; Goetzl, Sebastian; Jeoung, Jae‐Hun; Léger, Christophe; Dementin, Sébastien; Fourmond, Vincent; Dobbek, Holger
• Is Part Of: Angewandte Chemie international edition. Volume 56:Issue 48(2017)
• Page Start: 15466
• Page End: 15469
• Publication Date: 2017-11-02
• Subjects: activation energy -- carbon dioxide reduction -- diffusion-limited enzyme -- electrochemistry -- O2 resistance; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201709261
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: CO dehydrogenases (CODHs) catalyse the reversible conversion between CO and CO2 . Genomic analysis indicated that the metabolic functions of CODHs vary. The genome of Carboxydothermus hydrogenoformans encodes five CODHs (CODH‐I–V), of which CODH‐IV is found in a gene cluster near a peroxide‐reducing enzyme. Our kinetic and crystallographic experiments reveal that CODH‐IV differs from other CODHs in several characteristic properties: it has a very high affinity for CO, oxidizes CO at diffusion‐limited rate over a wide range of temperatures, and is more tolerant to oxygen than CODH‐II. Thus, our observations support the idea that CODH‐IV is a CO scavenger in defence against oxidative stress and highlight that CODHs are more diverse in terms of reactivity than expected. Abstract : Scavenger hunt : CO dehydrogenases (CODHs) catalyse the reversible conversion between CO and CO2 . CODH‐IV is shown to differ from other CODHs. In particular, it acts as a CO scavenger in defence against oxidative stress, highlighting that CODHs are more diverse in terms of reactivity than expected.