Functional asymmetry and electron flow in the bovine respirasome
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...
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doaj-a1e3a801e2114ff9aade6f7770f3612d2021-05-05T00:40:43ZengeLife Sciences Publications LtdeLife2050-084X2016-11-01510.7554/eLife.21290Functional asymmetry and electron flow in the bovine respirasomeJoana S Sousa0Deryck J Mills1Janet Vonck2https://orcid.org/0000-0001-5659-8863Werner Kühlbrandt3https://orcid.org/0000-0002-2013-4810Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, GermanyDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, GermanyDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, GermanyDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, GermanyRespirasomes 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.https://elifesciences.org/articles/21290Bos tauruscryo-EMmitochondriarespiratory chainsupercomplex |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Joana S Sousa Deryck J Mills Janet Vonck Werner Kühlbrandt |
spellingShingle |
Joana S Sousa Deryck J Mills Janet Vonck Werner Kühlbrandt Functional asymmetry and electron flow in the bovine respirasome eLife Bos taurus cryo-EM mitochondria respiratory chain supercomplex |
author_facet |
Joana S Sousa Deryck J Mills Janet Vonck Werner Kühlbrandt |
author_sort |
Joana S Sousa |
title |
Functional asymmetry and electron flow in the bovine respirasome |
title_short |
Functional asymmetry and electron flow in the bovine respirasome |
title_full |
Functional asymmetry and electron flow in the bovine respirasome |
title_fullStr |
Functional asymmetry and electron flow in the bovine respirasome |
title_full_unstemmed |
Functional asymmetry and electron flow in the bovine respirasome |
title_sort |
functional asymmetry and electron flow in the bovine respirasome |
publisher |
eLife Sciences Publications Ltd |
series |
eLife |
issn |
2050-084X |
publishDate |
2016-11-01 |
description |
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. |
topic |
Bos taurus cryo-EM mitochondria respiratory chain supercomplex |
url |
https://elifesciences.org/articles/21290 |
work_keys_str_mv |
AT joanassousa functionalasymmetryandelectronflowinthebovinerespirasome AT deryckjmills functionalasymmetryandelectronflowinthebovinerespirasome AT janetvonck functionalasymmetryandelectronflowinthebovinerespirasome AT wernerkuhlbrandt functionalasymmetryandelectronflowinthebovinerespirasome |
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1721476179770212352 |