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

Thioredoxin reductase (TRR), a member of the pyridine nucleotide-disulfide oxidoreductase family of flavoenzymes, undergoes two sequential thiol-disulfide interchange reactions with thioredoxin during catalysis. In order to assess the catalytic role of each nascent thiol of the active site disulfide...

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Veröffentlicht in:The Journal of biological chemistry 1989-02, Vol.264 (5), p.2656-2664
Hauptverfasser: Prongay, A J, Engelke, D R, Williams, C H
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Sprache:eng
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