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. 2022 Jan 18;204(1):e00421-21. doi: 10.1128/JB.00421-21

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Copyright © 2022 Nasher et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license.

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FIG 5 — Reductase activity of purified recombinant MdaB and NfrA. (a) UV-visible spectrum of MdaB showing characteristic flavin cofactor absorbance peaks; inset shows the magnified view of the absorption spectra. (b) Traces of quinone reductase assay with purified MdaB_his6 and NADPH (average of triplicates). (c) Specific activity of MdaB_his6 with quinone substrates calculated from initial rate (arrow indicates <0). (d) Riboflavin reductase activity of purified NrfA_his6 showing preference for NADPH over NADH. (e) Specific activity of NrfA_his6 with flavin substrates and NADPH. (f) Direct measurement of riboflavin reduction by NrfA_his6 and NADPH anaerobically by following the riboflavin absorbance maximum of 445 nm. All assays were performed at pH ∼7.5.