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. 2021 Apr 13;4:467. doi: 10.1038/s42003-021-01987-5

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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 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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Fig. 4 — A Spectral change upon ferric hemin addition. Inset, titration curve of hemin binding to apo-PefR measured at 412 nm. A dimer of PefR binds two hemes, and the stoichiometry is 1:1 when considering a monomer PefR. B ITC of heme binding to apo-PefR. Top panel, differential heating power versus time. Lower panel, integrated and normalized heat of reaction versus the molar ratio. Experimental data are shown by black squares. Red lines show the best fit to the binding isotherm using a one-site binding model. C Optical absorption spectra of PefR (5 μM) in Fe³⁺, Fe³⁺CN⁻ (left panel), and Fe³⁺, Fe²⁺, and Fe²⁺CO (right panel) in 40 mM Tris/HCl (pH 7.4) and 500 mM NaCl.