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. 2017 Aug 10;7:7747. doi: 10.1038/s41598-017-07930-1

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© The Author(s) 2017

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/.

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Structure of respiratory complex I embedded in lipid-solvent environment. The membrane-embedded antiporter-type subunits Nqo12–14 are shown in orange, blue and magenta, respectively. Nqo8 (green), Nqo7, Nqo10 and Nqo11 (violet-indigo) are also displayed along with the hydrophilic subunits Nqo6 (light blue) and Nqo4 (pink) that form the Q-binding site scaffold. Q (purple) binds in a buried binding site. All other hydrophilic subunits are shown in grey. Covalently-bound FeS clusters (pink-yellow spheres), and FMN (orange) at the terminal end of the hydrophilic domain are also shown. NADH binds next to FMN and acts as a direct donor of two electrons to the latter. The region studied in this work is marked by a thick black box, and is shown to atomic details in the inset (box with dotted lines). The residues discussed in this work are also marked (inset).