CODH-IV: A High-Efficiency CO-Scavenging CO Dehydrogenase with Resistance to O2.
Lilith DomnikMeriem MerrouchSebastian GoetzlJae-Hun JeoungChristophe LégerSébastien DementinVincent FourmondHolger DobbekPublished in: Angewandte Chemie (International ed. in English) (2017)
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.