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TitleThe -II terminal oxidase employs a carboxylate shift mechanism.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 123, Issue 11, Page e2515348123, Year 2026
Publish dateMar 17, 2026
AuthorsTerezia Kovalova / Mateusz Janczak / Ana P Gamiz-Hernandez / Daniel Lundin / Soni Sharma / Johanna Vilhjálmsdóttir / Dan Sjöstrand / Ville R I Kaila / Martin Högbom / Pia Ädelroth /
PubMed AbstractCytochrome is a terminal oxidase expressed under low oxygen conditions and central for the survival of many pathogens. Here, we characterize the cyt -II from , a member of a hitherto uncharacterized ...Cytochrome is a terminal oxidase expressed under low oxygen conditions and central for the survival of many pathogens. Here, we characterize the cyt -II from , a member of a hitherto uncharacterized evolutionary group (qOR-2) of oxidases, by combining biochemical studies with cryo-electron microscopy (cryo-EM), and multiscale simulations. Overexpressing the operon in its native host led to production of a highly active -II ( = 30 e s) that together with a high-resolution (2.8 Å) cryo-EM structure and multiscale simulations reveal unique proton pathways and oxygen channels responsible for its function. We propose that a pH-dependent molecular switch, involving coordination changes of heme and surrounding bulky residues regulate substrate access into the active site. Taken together, our findings provide detailed mechanistic insight of qOR-2 type oxidases, and a basis for understanding the evolution of the superfamily.
External linksProc Natl Acad Sci U S A / PubMed:41805574 / PubMed Central
MethodsEM (single particle)
Resolution2.8 Å
Structure data

53529

9r2g

EMDB-53529, PDB-9r2g:
Cytochrome bd II oxidase qOR-2 type from Mycobacterium smegmatis
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

ChemComp-HDD:
CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE

ChemComp-HEB:
HEME B/C

ChemComp-MQ9:
MENAQUINONE-9

ChemComp-HOH:
WATER

Source
  • mycolicibacterium smegmatis (bacteria)
KeywordsELECTRON TRANSPORT / MEMBRANE PROTEIN / ACTINOBACTERIA

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