Mechanism and structure of thioredoxin reductase from Escherichia coli

@article{Williams1995MechanismAS,
  title={Mechanism and structure of thioredoxin reductase from Escherichia coli},
  author={Charles H. Williams},
  journal={The FASEB Journal},
  year={1995},
  volume={9},
  pages={1267 - 1276},
  url={https://api.semanticscholar.org/CorpusID:26055087}
}
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.
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147 Citations
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Background Citations
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147 Citations

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50 References

Oxidation-reduction properties of Escherichia coli thioredoxin reductase altered at each active site cysteine residue.

The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates.

Characterization of the active center of thioredoxin reductase.

Kinetics of electron transfer from thioredoxin reductase to thioredoxin.

The reduction of Escherichia coli thiOREDoxin by thioredoxin reductase was studied by stopped-flow spectrophotometry, indicating that complex formation was rapid and occurred during the dead time of the instrument.

Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis.

The results suggest that thioredoxin reductase must undergo conformational changes during enzyme catalysis, and no direct evidence is available as yet for such conformational change.

Characterization of two active site mutations of thioredoxin reductase from Escherichia coli.

The finding of activity in the mutants indicates that the remaining thiol can carry out interchange with the disulfide of thioredoxin, and the resulting mixed disulfides can be reduced by NADPH via the flavin.

The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid.

Evidence for direct interaction between cysteine 138 and the flavin in thioredoxin reductase. A study using flavin analogs.

The flavoenzyme thioredoxin reductase from Escherichia coli contains an oxidation-reduction active disulfide made up of Cys135 and Cys138, which has absorbance and fluorescence spectral properties similar to the oxidized form of wild type apothiored toxin reduct enzyme reconstituted with 1-deaza-FAD.

Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases.

The streptococcal flavoprotein NADH oxidase. I. Evidence linking NADH oxidase and NADH peroxidase cysteinyl redox centers.

Thiol assays of the NADH oxidase, reduced anaerobically with 1 eq of NADH/FAD prior to denaturation, are consistent with the presence of a single redox-active cysteinyl residue/subunit, which provides further evidence for a fundamental structural connection between flavin-dependent NADh oxidase and peroxidase functions.