TY  - JOUR
A1  - Sousa, Joana Sofia de
A1  - Calisto, Filipa
A1  - Langer, Julian David
A1  - Mills, Deryck J.
A1  - Refojo, Patrícia N.
A1  - Teixeira, Miguel
A1  - Kühlbrandt, Werner
A1  - Vonck, Janet
A1  - Pereira, Manuela
T1  - Structural basis for energy transduction by respiratory alternative complex III
T2  - Nature Communications
N2  - 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.
KW  - Bioenergetics
KW  - Cryoelectron microscopy
KW  - Oxidoreductases
Y1  - 2018
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/46603
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-466034
SN  - 2041-1723
N1  - 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/.
VL  - 9
IS  - 1, Art. 1728
SP  - 1
EP  - 10
PB  - Nature Publishing Group UK
CY  - [London]
ER  -