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. 2017 May 11;7:1757. doi: 10.1038/s41598-017-01840-y

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© The Author(s) 2017

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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Mo K-edge X-ray absorption near-edge spectra of NT-26 arsenite oxidase. The as-isolated enzyme is shown in a () with the same form of the enzyme after addition of 5 mM arsenite (). The two traces overlay almost completely within the width of the line, showing that there are no significant changes in the Mo site arising from addition of substrate. The effects of addition of 5 mM (final) ferricyanide solution are shown in b, with the as-isolated protein () verses the ferricyanide-oxidized enzyme (). c shows the spectrum of ferricyanide-oxidized enzyme () compared with that of arsenite-reduced enzyme ().

Inline graphic — Mo K-edge X-ray absorption near-edge spectra of NT-26 arsenite oxidase. The as-isolated enzyme is shown in a () with the same form of the enzyme after addition of 5 mM arsenite (). The two traces overlay almost completely within the width of the line, showing that there are no significant changes in the Mo site arising from addition of substrate. The effects of addition of 5 mM (final) ferricyanide solution are shown in b, with the as-isolated protein () verses the ferricyanide-oxidized enzyme (). c shows the spectrum of ferricyanide-oxidized enzyme () compared with that of arsenite-reduced enzyme ().