Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase.

@article{Lennon2000TwistsIC,
  title={Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase.},
  author={Brett W. Lennon and C. Howard Williams and Martha L. Ludwig},
  journal={Science},
  year={2000},
  volume={289 5482},
  pages={
          1190-4
        }
}
In thioredoxin reductase (TrxR) from Escherichia coli, cycles of reduction and reoxidation of the flavin adenine dinucleotide (FAD) cofactor depend on rate-limiting rearrangements of the FAD and NADPH (reduced form of nicotinamide adenine dinucleotide phosphate) domains. We describe the structure of the flavin-reducing conformation of E. coli TrxR at a resolution of 3.0 angstroms. The orientation of the two domains permits reduction of FAD by NADPH and oxidation of the enzyme dithiol by the… Expand
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