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TitleQuinone extraction drives atmospheric carbon monoxide oxidation in bacteria.
Journal, issue, pagesNat Chem Biol, Vol. 21, Issue 7, Page 1058-1068, Year 2025
Publish dateJan 29, 2025
AuthorsAshleigh Kropp / David L Gillett / Hari Venugopal / Miguel A Gonzálvez / James P Lingford / Surbhi Jain / Christopher K Barlow / Jie Zhang / Chris Greening / Rhys Grinter /
PubMed AbstractDiverse bacteria and archaea use atmospheric CO as an energy source for long-term survival. Bacteria use [MoCu]-CO dehydrogenases (Mo-CODH) to convert atmospheric CO to carbon dioxide, transferring ...Diverse bacteria and archaea use atmospheric CO as an energy source for long-term survival. Bacteria use [MoCu]-CO dehydrogenases (Mo-CODH) to convert atmospheric CO to carbon dioxide, transferring the obtained electrons to the aerobic respiratory chain. However, it is unknown how these enzymes oxidize CO at low concentrations and interact with the respiratory chain. Here, we use cryo-electron microscopy and structural modeling to show how Mo-CODH (CoxSML) from Mycobacterium smegmatis interacts with its partner, the membrane-bound menaquinone-binding protein CoxG. We provide electrochemical, biochemical and genetic evidence that Mo-CODH transfers CO-derived electrons to the aerobic respiratory chain through CoxG. Lastly, we show that Mo-CODH and CoxG genetically and structurally associate in diverse bacteria and archaea. These findings reveal the basis of the biogeochemically and ecologically important process of atmospheric CO oxidation, while demonstrating that long-range quinone transport is a general mechanism of energy conservation, which convergently evolved on multiple occasions.
External linksNat Chem Biol / PubMed:39881213 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.5 - 1.85 Å
Structure data

42164

8uem

EMDB-42164, PDB-8uem:
The CryoEM structure of the high affinity Carbon monoxide dehydrogenase from Mycobacterium smegmatis
Method: EM (single particle) / Resolution: 1.85 Å

PDB-8uds:
The Crystal Structure of CoxG from M. smegmatis, minus lipid anchoring C-terminus.
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-CUN:
CU(I)-S-MO(IV)(=O)OH CLUSTER

ChemComp-MCN:
PTERIN CYTOSINE DINUCLEOTIDE

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

Source
  • mycolicibacterium smegmatis mc2 155 (bacteria)
KeywordsELECTRON TRANSPORT / Menaquinone Binding / Lipid Anchored / Carbon monoxide dehydrogenase / SRPBCC family protein / OXIDOREDUCTASE / MoCu / Mycobacterium smegmatis / High affinity / trace gas scavenging

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