Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: evidence that cysteine-138 functions to initiate dithiol-disulfide interchange and to accept the reducing equivalent from reduced flavin. [electronic resource]
Producer: 19980901Description: 1441-50 p. digitalISSN:- 0961-8368
- Cysteine -- genetics
- Disulfides -- chemistry
- Dithionite -- chemistry
- Dithionitrobenzoic Acid -- chemistry
- Dithiothreitol -- chemistry
- Escherichia coli -- enzymology
- Flavin-Adenine Dinucleotide -- chemistry
- Hydrogen-Ion Concentration
- Mutagenesis, Site-Directed
- NADP -- chemistry
- Osmolar Concentration
- Oxidation-Reduction
- Protein Conformation
- Protein Engineering
- Spectrometry, Fluorescence
- Structure-Activity Relationship
- Sulfhydryl Compounds -- chemistry
- Thioredoxin-Disulfide Reductase -- chemistry
- Thioredoxins -- chemistry
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Publication Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
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