Thioredoxin reductase two modes of catalysis have evolved.

@article{Williams2000ThioredoxinRT,
  title={Thioredoxin reductase two modes of catalysis have evolved.},
  author={C. Williams and L. Arscott and S. Müller and B. Lennon and M. Ludwig and P. F. Wang and D. M. Veine and K. Becker and R. Schirmer},
  journal={European journal of biochemistry},
  year={2000},
  volume={267 20},
  pages={
          6110-7
        }
}
Thioredoxin reductase (EC 1.6.4.5) is a widely distributed flavoprotein that catalyzes the NADPH-dependent reduction of thioredoxin. Thioredoxin plays several key roles in maintaining the redox environment of the cell. Like all members of the enzyme family that includes lipoamide dehydrogenase, glutathione reductase and mercuric reductase, thioredoxin reductase contains a redox active disulfide adjacent to the flavin ring. Evolution has produced two forms of thioredoxin reductase, a protein in… Expand
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  • C. Williams
  • Chemistry, Medicine
  • European journal of biochemistry
  • 2000
TLDR
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Structure and stability of a thioredoxin reductase from Sulfolobus solfataricus: a thermostable protein with two functions.
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TLDR
The flavoprotein disulfide reductases represent a family of enzymes that show high sequence and structural homology and selection of the particular nonflavin redox center and utilization of a second, or even a third, nonfl Gavin redoxcenter in some cases presumably represents the most efficient strategy for reduction of the individual substrate. Expand
High-resolution structures of oxidized and reduced thioredoxin reductase from Helicobacter pylori.
TLDR
The overall surface charge distribution in these proteins is conserved and that residue substitutions that change the shape of the binding surface may account for the species-specific recognition of thioredoxin by TrxR. Expand
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  • C. Williams
  • Chemistry, Medicine
  • FASEB journal : official publication of the Federation of American Societies for Experimental Biology
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TLDR
This paper attempts to correlate the structure of thioredoxin reductase with a considerable body of mechanistic data and to arrive at a mechanism consistent with both and envisage the path of reducing equivalents in catalysis by thioreductase. Expand
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TLDR
The results suggest that wild type and each altered enzyme exists in a unique equilibrium of conformers, and it is proposed that the third phase of the reductive half-reaction represents a flavin reduction event largely limited by the conformational change proposed in the structural work. Expand
Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5 A resolution.
TLDR
The first structure of a eukaryotic thioredoxin reductase is determined, from the plant Arabidopsis thaliana, at 2.5 A resolution, structurally similar to that of the Escherichia coli enzyme, and most differences occur in the loops. Expand
Thioredoxin reductase from Escherichia coli: Evidence of restriction to a single conformation upon formation of a crosslink between engineered cysteines
TLDR
Evidence is consistent with the hypothesis that thioredoxin reductase requires a conformational change to complete catalysis and the crosslink in the CC‐mutant was intramolecular. Expand
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TLDR
It has been proposed that a large conformational change is required in catalysis by TrT in order to visualize a complete pathway for reduction of equivalents and it was reported previously that TrR C135S can form a charge transfer complex in the presence of ammonium cation in which the donor is the remaining thiolate of Cys138. Expand
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TLDR
In its physiological, NADPH-reduced form, the enzyme is strongly inhibited by organic gold compounds that are widely used in the treatment of rheumatoid arthritis; for auranofin, the K i was 4 nm when measured in the presence of 50 μmthioredoxin. Expand
AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase.
TLDR
A group of bacterial flavoproteins related to thioredoxin reductase contain an additional approximately 200-amino-acid domain including a redox-active disulfide center at their N-termini which catalyze the pyridine-nucleotide-dependent reduction of cysteine-based peroxidases which in turn reduce H2O2 or organic hydroperoxides. Expand
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TLDR
The structure of the flavin-reducing conformation of E. coli TrxR is described and it is demonstrated that switching between the two conformations involves a "ball-and-socket" motion in which the pyridine nucleotide-binding domain rotates by 67 degrees. Expand
The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli.
TLDR
Three lines of evidence indicate that the mechanism of human thioredoxin reductase is like the mechanisms of lipoamide dehydrogenase and glutathione reduct enzyme and differs fundamentally from the mechanism from E. coli thiOREDoxin reducase. Expand
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TLDR
It is shown that E. coli thioredoxin reductase lacks the domain that provides the dimer interface in glutathione reductases, and forms a completely different dimeric structure, which suggests that these enzymes diverged from an ancestral nucleotide-binding protein and acquired their disulphide reduct enzyme activities independently. Expand
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