In-cell architecture of the mitochondrial respiratory chain
Mitochondria regenerate adenosine triphosphate (ATP) through oxidative phosphorylation. This process is carried out by five membrane-bound complexes collectively known as the respiratory chain, working in concert to transfer electrons and pump protons. The precise organization of these complexes in native cells is debated. We used in situ cryo-electron tomography to visualize the native structures and organization of several major mitochondrial complexes in <i>Chlamydomonas reinhardtii</i> cells. ATP synthases and respiratory complexes segregate into curved and flat crista membrane domains, respectively. Respiratory complexes I, III, and IV assemble into a respirasome supercomplex, from which we determined a native 5-angstrom (Å) resolution structure showing binding of electron carrier cytochrome <i>c</i>. Combined with single-particle cryo-electron microscopy at 2.4-Å resolution, we model how the respiratory complexes organize inside native mitochondria.
Authors
- Sagar Khavnekar (ORCID: https://orcid.org/0000-0003-2020-3561)
- Florent Waltz (ORCID: https://orcid.org/0000-0002-2251-3363)
- Martin Obr (ORCID: https://orcid.org/0000-0003-1756-6564)
- Abhay Kotecha (ORCID: https://orcid.org/0000-0002-4480-5439)
- Lorenz Lamm (ORCID: https://orcid.org/0000-0003-0698-7769)
- Benjamin D. Engel (ORCID: https://orcid.org/0000-0002-0941-4387)
- Thalia Salinas‐Giegé (ORCID: https://orcid.org/0000-0003-0220-4173)
- Xianjun Zhang (ORCID: https://orcid.org/0000-0003-3554-780X)
- Ricardo D. Righetto (ORCID: https://orcid.org/0000-0003-4247-4303)
- Ron Kelley
Institutions
- Centre National de la Recherche Scientifique (FR)
- St. Jude Children's Research Hospital (US)
- University of Basel (CH)
- Helmholtz Zentrum München (DE)
- Thermo Fisher Scientific (Netherlands) (NL)
- Institut de Biologie Moléculaire des Plantes (FR)
- Max Planck Institute of Biochemistry (DE)
- Université de Strasbourg (FR)
Publication Details
- Journal
- Science
- Published
- 2025-03-20
- DOI
- https://doi.org/10.1126/science.ads8738
- Citations
- 49
- Primary Topic
- ATP Synthase and ATPases Research
- Type
- article
- Field-Weighted Citation Impact
- 38.69