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. 2022 Dec 30;9(1):142–156. doi: 10.1038/s41477-022-01308-6

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© The Author(s) 2022

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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Extended Data Fig. 2 — a, Overview from the matrix side. b, Cofactors involved in respiratory electron transport. Complex I: FMN (Flavin mononucleotide), N1a, N1b, N2, N3, N4, N5, N6a, N6b (8 FeS clusters) and C1-Q (ubiquinol/ubiquinone at the Q reduction site). Complex III₂: two copies each of heme b_H, b_L and c₁, Rieske FeS, plus ubiquinone/ubiquinol at the Q_o and Q_i sites. c, Other cofactors: PP (S-acyl-4ʼ-phosphopantetheine bound to SDAP1 and SDAP2), CoA-X (Butyryl-or Crotonyl-Coenzym A bound to γCA), and NADPH bound to the 39 kDA subunit. d, Bound metal ions. e, Lipids and detergent molecules, with numbers of copies in round brackets. PA, phosphatidic acid (11); PC, phosphatidylcholine (9); PE, phosphatidylethanolamine (14); PG, phosphatidylglycerol (10); CL, cardiolipin (8); GDN, glyco-diosgenin (10); Q, ubiquinone/ubiquinol (not bound in the Q reduction site of complex I or in the Q_o and Q_i sites of complex III₂). Densities and models of selected cofactors, metal ions and lipids are highlighted.