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The respiratory supercomplex from C. glutamicum.

Agnes Moe1, Terezia Kovalova1, Sylwia Król1

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Summary
This summary is machine-generated.

Researchers elucidated the structure of the respiratory supercomplex (CIII2CIV2) in Corynebacterium glutamicum using cryo-EM. This reveals key menaquinone binding sites and proton transfer pathways essential for aerobic respiration.

Keywords:
ActinobacteriaBioenergeticsElectron transfercytochrome bc(1)cytochrome c oxidaseelectrochemical potentialenergy conservationmembrane proteinproton transferrespiration

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Corynebacterium glutamicum is an aerobic Gram-positive bacterium.
  • Respiratory complexes III (CIII2) and IV (CIV2) form a supercomplex (CIII2CIV2) in Actinobacteria, including Mycobacterium tuberculosis.
  • This supercomplex is crucial for menaquinol oxidation and oxygen reduction to water.

Purpose of the Study:

  • To determine the high-resolution structure of the C. glutamicum CIII2CIV2 supercomplex.
  • To elucidate the molecular mechanisms of menaquinone binding and electron transfer within the supercomplex.
  • To identify the structural basis for proton transfer pathways.

Main Methods:

  • Isolation of the C. glutamicum CIII2CIV2 supercomplex.
  • Cryo-electron microscopy (cryo-EM) for structural determination.
  • High-resolution structural analysis at 2.9 Å.

Main Results:

  • The cryo-EM structure reveals a central CIII2 dimer flanked by two CIV complexes.
  • Identified menaquinone binding sites (QN and QP) within CIII and an additional menaquinone near heme bL.
  • Revealed a di-heme cytochrome c subunit connecting CIII and CIV, with the Rieske iron-sulfur protein positioned near heme bL.
  • Discovered a complex cytoplasmic substructure facilitating proton transfer into CIV.

Conclusions:

  • The determined structure provides unprecedented insight into the CIII2CIV2 supercomplex organization in C. glutamicum.
  • The findings clarify the roles of menaquinone binding and electron transfer pathways in aerobic respiration.
  • The study reveals the structural basis for proton translocation, essential for energy conservation.