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CODH‐IV: A High‐Efficiency CO‐Scavenging CO Dehydrogenase with Resistance to O 2
Author(s) -
Domnik Lilith,
Merrouch Meriem,
Goetzl Sebastian,
Jeoung JaeHun,
Léger Christophe,
Dementin Sébastien,
Fourmond Vincent,
Dobbek Holger
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.201709261
Subject(s) - chemistry , reactivity (psychology) , carbon monoxide dehydrogenase , scavenger , enzyme , stereochemistry , biochemistry , catalysis , radical , carbon monoxide , medicine , alternative medicine , pathology
CO dehydrogenases (CODHs) catalyse the reversible conversion between CO and CO 2 . 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.