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. 2015 Oct 1;6:1073. doi: 10.3389/fmicb.2015.01073

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Copyright © 2015 Riedel, Mehnert, Paul, Westphal, van Berkel and Tischler.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Thermal stability of purified OYERo2 () and OYERo2a (). (A,B) Thermal stability was measured applying the standard assay. Protein was incubated in 50 mM phosphate buffer (pH 7.1) at various temperatures (1–50°C) and added to the assay in a final concentration of 30 nM. (C) Inactivation at 32°C with constant high protein concentrations of 7 μM (hc) and varying NADPH concentrations: 1 mM (red; continuous lines) and 0 mM (ox; dashed lines). (D) Inactivation at 32°C with various protein concentrations under reducing conditions: 7 μM protein and 1 mM NADPH (hc; continuous lines) and 30 nM protein and 0.14 mM NADPH (lc, dashed lines).

Inline graphic — Thermal stability of purified OYERo2 () and OYERo2a (). (A,B) Thermal stability was measured applying the standard assay. Protein was incubated in 50 mM phosphate buffer (pH 7.1) at various temperatures (1–50°C) and added to the assay in a final concentration of 30 nM. (C) Inactivation at 32°C with constant high protein concentrations of 7 μM (hc) and varying NADPH concentrations: 1 mM (red; continuous lines) and 0 mM (ox; dashed lines). (D) Inactivation at 32°C with various protein concentrations under reducing conditions: 7 μM protein and 1 mM NADPH (hc; continuous lines) and 30 nM protein and 0.14 mM NADPH (lc, dashed lines).