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. 2019 Jul 23;9:10694. doi: 10.1038/s41598-019-47018-6

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© The Author(s) 2019

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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Interactors of UQCRC1 – UQCRC2 and CYC1. (A) – Surface represented UQCRC1 (pink) is shown to have tangible interactions with UQCRC2 (blue), CYC (yellow), UQCRFS1 (orange), UQCRQ (violet), UQCR10 (purple) and UQCR11 (cyan). (B) – H-bond analysis between UQCRC1 and UQCRC2 shows ~10 bond decrease in the oxidized form (red) compared to control (green) state. (C) – Interaction between the C-terminal regions of the CYC1 with UQCRC1 is mediated by Glu139, His243 and Asn235 in the former (represented in yellow sticks) with the residues Lys241, Arg238 and Lys226 in the latter (represented in pink sticks). Post-oxidation, the residues Arg238 and Lys226 of CYC1 were found to drift away from UQCRC1 breaking the bonds. (D) - H-bond analysis between UQCRC1 and CYC1 shows two-thirds decrease in the hydrogen bond contacts between the subunits explained due to loss of interactions as in C.