Structural basis for energy transduction by respiratory alternative complex III

  • Electron transfer in respiratory chains generates the electrochemical potential that serves as energy source for the cell. Prokaryotes can use a wide range of electron donors and acceptors and may have alternative complexes performing the same catalytic reactions as the mitochondrial complexes. This is the case for the alternative complex III (ACIII), a quinol:cytochrome c/HiPIP oxidoreductase. In order to understand the catalytic mechanism of this respiratory enzyme, we determined the structure of ACIII from Rhodothermus marinus at 3.9 Å resolution by single-particle cryo-electron microscopy. ACIII presents a so-far unique structure, for which we establish the arrangement of the cofactors (four iron–sulfur clusters and six c-type hemes) and propose the location of the quinol-binding site and the presence of two putative proton pathways in the membrane. Altogether, this structure provides insights into a mechanism for energy transduction and introduces ACIII as a redox-driven proton pump.
Metadaten
Author:Joana Sofia de Sousa, Filipa Calisto, Julian David Langer, Deryck J. Mills, Patrícia N. Refojo, Miguel Teixeira, Werner Kühlbrandt, Janet Vonck, Manuela Pereira
URN:urn:nbn:de:hebis:30:3-466034
DOI:https://doi.org/10.1038/s41467-018-04141-8
ISSN:2041-1723
Pubmed Id:https://pubmed.ncbi.nlm.nih.gov/29712914
Parent Title (English):Nature Communications
Publisher:Nature Publishing Group UK
Place of publication:[London]
Document Type:Article
Language:English
Year of Completion:2018
Date of first Publication:2018/04/30
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2018/06/14
Tag:Bioenergetics; Cryoelectron microscopy; Oxidoreductases
Volume:9
Issue:1, Art. 1728
Page Number:10
First Page:1
Last Page:10
Note:
Rights and permissions: Open Access: This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
HeBIS-PPN:433825936
Institutes:Biochemie, Chemie und Pharmazie / Biochemie und Chemie
Angeschlossene und kooperierende Institutionen / MPI für Biophysik
Angeschlossene und kooperierende Institutionen / MPI für Hirnforschung
Dewey Decimal Classification:6 Technik, Medizin, angewandte Wissenschaften / 61 Medizin und Gesundheit / 610 Medizin und Gesundheit
Sammlungen:Universitätspublikationen
Licence (German):License LogoCreative Commons - Namensnennung 4.0