| Literature DB >> 29024326 |
Lilith Domnik1, Meriem Merrouch2, Sebastian Goetzl1, Jae-Hun Jeoung1, Christophe Léger2, Sébastien Dementin2, Vincent Fourmond2, Holger Dobbek1.
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.Entities:
Keywords: O2 resistance; activation energy; carbon dioxide reduction; diffusion-limited enzyme; electrochemistry
Year: 2017 PMID: 29024326 DOI: 10.1002/anie.201709261
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336