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. 2018 May 25;8:8121. doi: 10.1038/s41598-018-26445-x

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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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Time course of reoxidation of Phe397 variants with O₂. (a) F397Y spectra measured at 0.002, 0.01, 0.02, 0.03, 0.04, 0.05, 0.06, 0.07, 0.08, 0.5, 1 and 1.5 s after mixing. (b) F397W recorded at 0.001, 0.005, 0.01, 0.02, 0.03, 0.04, 0.05, 0.06, 0.07, 0.08, 0.09, 0.1, 0.18 and 0.2 s. (c) F397A recorded at 0.002, 0.01, 0.02, 0.03, 0.04, 0.05, 0.06, 0.07, 0.08, 0.09, 0.5, 1, and 1.5 s. (d) F397L recorded at 0.002, 0.01, 0.02, 0.03, 0.04, 0.05, 0.06, 0.07, 0.08, 0.09, 0.1, 0.3, 0.5, 0.7, 0.9 and 1 s. Enzyme (~10 µM) reactions with O₂ (136 μM) were performed in 50 mM sodium phosphate, pH 6.0, at 12 °C. Dashed lines correspond to the reduced enzymes. Insets show the evolution of species A, B and C after data fitting to a two-step process. The estimated k_obs for each phase is represented in each panel.