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Article

Structure requirements for disulfide bridge sulfitolysis of oxidized Escherichia coli thioredoxin studied by fluorescence spectroscopy.

European journal of biochemistry - 15 Jul 1994

Häberlein I

Abstract excerpt

Sulfitolysis of wild-type and four mutated Escherichia coli thioredoxins ([D26A]thioredoxin, [P34H]thioredoxin, [K36E]thioredoxin and endo-Arg33a-thioredoxin) has been investigated at millimolar concentrations of sulfite in the absence of protein-denaturing agents by fluorescence spectroscopy. Sulfitolysis of the single disulfide bridge of these proteins is associated with an increase in fluorescence emissions at...

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PMID: 8055916
DOI: 10.1111/j.1432-1033.1994.tb19015.x

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