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Article

Conformation, stability, and active-site cysteine titrations of Escherichia coli D26A thioredoxin probed by Raman spectroscopy.

Protein science : a publication of the Protein Society - 1 Jan 1998

Vohník S, Hanson C, Tuma R, Fuchs J A, Woodward C, Thomas G J

Abstract excerpt

The active-site cysteines (Cys 32 and Cys 35) of Escherichia coli thioredoxin are oxidized to a disulfide bridge when the protein mediates substrate reduction. In reduced thioredoxin, Cys 32 and Cys 35 are characterized by abnormally low pKa values. A conserved side chain, Asp 26, which is sterically accessible to the active site, is also essential to oxidoreductase activity. pKa values governing cysteine...

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PMID: 9514274
DOI: 10.1002/pro.5560070120
PMCID: PMC2143819

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