Journal of Molecular Biology
Regular ArticleCrystal Structure of Escherichia coli Thioredoxin Reductase Refined at 2 Å Resolution: Implication for a Large Conformational Change during Catalysis
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Overview of structurally homologous flavoprotein oxidoreductases containing the low M<inf>r</inf> thioredoxin reductase-like fold – A functionally diverse group
2021, Archives of Biochemistry and BiophysicsCitation Excerpt :An intriguing feature of oxidized IruO/TrxR2 is that the conserved active site CXXC motif in the pyridine-nucleotide-binding domain is missing, placing the two above-mentioned cysteine residues in a hinge region between the cofactor-binding domains. This location does not place the redox-active disulfide close to the isoallozaxine ring of FAD (re-face), crucial for reduction of the disulfide by the reduced flavin, as seen in the TrxR FO conformation [36]. Also, as mentioned above, this Cys-pair is not conserved among homologous proteins in other Firmicutes, so the potential significance has to apply only for certain S. aureus strains.
Kinetic and structural insight into a role of the re-face Tyr328 residue of the homodimer type ferredoxin-NADP<sup>+</sup> oxidoreductase from Rhodopseudomonas palustris in the reaction with NADP<sup>+</sup>/NADPH
2020, Biochimica et Biophysica Acta - BioenergeticsCitation Excerpt :In this work, however, the residue located at the NADPH binding site in the NADP+/NADPH-binding domain was not mutated. The decrease in the KM and Kd values could be due to the changes in the accessibility of the nicotinamide ring portion of NADP+/NADPH to the re-face of the isoalloxazine ring portion because the utilized steady state assays monitor the perturbation of the FAD absorption bands (Fig. 1B), and the redox reaction involving H– transfer between NADPH and FAD, which requires stacking of the nicotine amide ring portion onto the isoalloxazine ring portion (Table 1) [40,41]. In the case of plant-type FNRs from Anabaena and pea, the interaction between the C-terminus Tyr residue and the isoalloxazine ring portion destabilizes the stacking of the nicotinamide ring portion of NADP+/NADPH onto the isoalloxazine ring, increasing the observed Kd and KM values, thereby enhancing the release of NADP+/NADPH, leading to an increase in the turnover rate [42–47].
A review on the druggability of a thiol-based enzymatic antioxidant thioredoxin reductase for treating filariasis and other parasitic infections
2020, International Journal of Biological MacromoleculesNovel starting points for fragment-based drug design against mycobacterial thioredoxin reductase identified using crystallographic fragment screening
2023, Acta Crystallographica Section D: Structural Biology