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. 2021 May 12;11:10143. doi: 10.1038/s41598-021-89575-9

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© The Author(s) 2021

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Creation of a catalytically inactive complex I variant. (a) Growth of wild-type P. denitrificans in succinate minimal media^40,41. Cells were grown with/without 10 mM taurine to induce NDH-2 expression and with/without 5 µM piericidin A to inhibit complex I and cell growth. (b) Comparison of the complex I flavin site activity (NADH:APAD⁺) of wild-type and the K232Q^Nqo13 variant measured in three different contexts. Membrane activities were measured using dNADH due to the expression of NDH-2 during cell growth. The specific activities have been normalized to the wild type activities; in membranes (0.527 ± 0.006 µmol min^–1 mg^–1, S.E.M. n = 3), purified CI (12.13 ± 0.14 µmol min^–1 mg^–1, S.E.M. n = 4), and proteoliposomes (10.71 ± 0.12 µmol min^–1 mg^–1, S.E.M. n = 3). (c) Comparison of the quinone reductase activity (Q₁₀ or DQ) of wild-type and the K232Q^Nqo13 variant measured in three different contexts. The specific activities have been normalized to the wild type activities (minus the average piericidin A insensitive rates) in membranes (2.41 ± 0.02 µmol min^–1 mg^–1, S.E.M. n = 3), purified enzyme (19.73 ± 0.058 µmol min^–1 mg^–1, S.E.M. n = 3), and proteoliposomes (41.45 ± 0.17 µmol min^–1 mg^–1, S.E.M. n = 3).