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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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Schematic diagram of postulated reaction sequence for Aio. The initial cis-dioxo Mo(VI) site (a) is destabilized by some 55 kJ/mol from the pterin-twist induced by the protein, and reacts with arsenite in the active site pocket via a transition state (b) containing arsenic bound to molybdenum via a linking oxygen. This then breaks down to form the reduced Mo(IV) enzyme site plus the reaction product arsenate, (c). The Mo(IV) form observed with bound arsenic in the presence of excess substrate (arsenite) is also shown in (d), which we suggest to be a dead-end complex of reduced enzyme and arsenite. The oxidized active site is regenerated from (c) through intramolecular electron transfer to the other redox active centers, and reaction with solvent water (not shown) to form the cis-dioxo active site a, completing the catalytic cycle.