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. 2022 Aug 11;11(8):1557. doi: 10.3390/antiox11081557

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© 2022 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Properties of H. influenzae MsrAB and accessory redox proteins (A) Schematic representation of the MsrAB reaction cycle. P_ox, P_red—generic oxidised or reduced protein, TrxR—Thioredoxin Reductase, Trx—thioredoxin, Trx_e—extracellular thioredoxin (B) Activity of rMsrAB and rMsrAB-Sp in an endpoint activity assay (C) Purified components of rMsrAB activity assay (D) Activity of the redox rMsrAB assay thioredoxin-based redox module using either insulin or oxidised glutathione (GSSG) as the artificial substrate. rMsrAB—recombinant methionine sulfoxide reductase activity, rTrxR—recombinant thioredoxin reductase, rTrx—recombinant thioredoxin, rTrx_e—recombinant extracellular thioredoxin. Structural representations of MsrAB and CcdA (Panel A) are based on Alphafold database models. Panel A was generated using BioRender.