Functional asymmetry and electron flow in the bovine respirasome

Elife. 2016 Nov 10;5:e21290. doi: 10.7554/eLife.21290.

Abstract

Respirasomes are macromolecular assemblies of the respiratory chain complexes I, III and IV in the inner mitochondrial membrane. We determined the structure of supercomplex I1III2IV1 from bovine heart mitochondria by cryo-EM at 9 Å resolution. Most protein-protein contacts between complex I, III and IV in the membrane are mediated by supernumerary subunits. Of the two Rieske iron-sulfur cluster domains in the complex III dimer, one is resolved, indicating that this domain is immobile and unable to transfer electrons. The central position of the active complex III monomer between complex I and IV in the respirasome is optimal for accepting reduced quinone from complex I over a short diffusion distance of 11 nm, and delivering reduced cytochrome c to complex IV. The functional asymmetry of complex III provides strong evidence for directed electron flow from complex I to complex IV through the active complex III monomer in the mammalian supercomplex.

Keywords: Bos taurus; biophysics; cryo-EM; mitochondria; respiratory chain; structural biology; supercomplex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Cryoelectron Microscopy
  • Electron Transport*
  • Mitochondria / enzymology*
  • Multienzyme Complexes / metabolism*
  • Multienzyme Complexes / ultrastructure*
  • Myocardium / enzymology

Substances

  • Multienzyme Complexes

Grant support

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.