6ELQ

Carbon Monoxide Dehydrogenase IV from Carboxydothermus hydrogenoformans

Summary for 6ELQ

• Entry DOI: 10.2210/pdb6elq/pdb
• Descriptor: Carbon Monoxide Dehydrogenase, IRON/SULFUR CLUSTER, FE(4)-NI(1)-S(5) CLUSTER with Oxygen, ... (4 entities in total)
• Functional Keywords: anaerobiosis, carbon dioxide, carbon monoxide, crystallization, iron, ligands, nickel, recombinant proteins, oxidoreductase
• Biological source: Carboxydothermus hydrogenoformans
• Total number of polymer chains: 3
• Total formula weight: 208053.85

Authors

Domnik, L.,Goetzl, S.,Jeoung, J.H.,Dobbek, H. (deposition date: 2017-09-29, release date: 2018-01-03, Last modification date: 2024-05-08)

Primary citation

Domnik, L.,Merrouch, M.,Goetzl, S.,Jeoung, J.H.,Leger, C.,Dementin, S.,Fourmond, V.,Dobbek, H.
CODH-IV: A High-Efficiency CO-Scavenging CO Dehydrogenase with Resistance to O2.
Angew. Chem. Int. Ed. Engl., 56:15466-15469, 2017

PubMed Abstract: CO dehydrogenases (CODHs) catalyse the reversible conversion between CO and CO . 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.

PubMed: 29024326
DOI: 10.1002/anie.201709261

Experimental method

X-RAY DIFFRACTION (2.52 Å)