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. 2017 Jul 20;8:16110. doi: 10.1038/ncomms16110

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Copyright © 2017, The Author(s)

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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(a) X-ray absorption near-edge spectra of IssA compared with a number of Fe–S proteins; a: IssA, b: linear 3Fe-4S cluster in human aconitase, c: P. furiosus 3Fe-4S ferredoxin and d: P. furiosus rubredoxin. The feature marked (*) in the IssA spectrum is due to a trace amount of sulfonate buffer. For both the S and Fe K-edge data, the IssA spectrum most resembles that of the linear 3Fe-4S cluster. (b) S and Fe K-edge EXAFS spectra, together with EXAFS Fourier transforms (S–Fe and Fe–S phase-corrected, respectively) showing experimental data (blue lines) together with best fits (red lines), the inset in the Fourier transform figure shows the structure used to compute the multiple scattering EXAFS. Best fits were computed with two S–Fe at 2.239(3) Å, σ²=0.0049(3) Å² and four Fe–S at 2.243(1) Å, σ²=0.0044(1) Å², two Fe····Fe at 2.704(1) Å, σ²=0.0032(1) Å² and two Fe····Fe at 5.408 Å and σ²=0.0064 Å².