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. 2018 Oct 19;8:15478. doi: 10.1038/s41598-018-33857-2

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© The Author(s) 2018

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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Model for electrogenic nitrate reduction in C. jejuni. The redox potential span between the MK/MKH₂ and the nitrate/nitrite couple is large enough to allow for a Qcr dependent electrogenic mechanism, given a typical transmembrane Δp of ~180 mV. The operation of the Qcr complex directly coupled to the NapAB enzyme gives a net transmembrane proton translocation of 2 H⁺ per 2e⁻ transferred from menaquinol. There is uncertainty about the precise route of electron transfer from the Qcr complex to NapB (dashed arrows) but the simplest mechanism would be direct transfer from haem 2 of QcrC to haem 1 of NapB. The role of NapG and NapH, which are known to be essential for nitrate respiration, is unclear. NapG may act in the electron transfer pathway itself or NapGH may act as a quinol dehydrogenase involved in a reductive maturation process e.g. for NapA. Black filled circles in QcrC and NapB represent the haems.