Fluorescence thioredoxin

Merola, R, Rigler, R., Holmgren, A., and Brochon, J-C., Picosecond tryptophan fluorescence of thioredoxin evidence for discrete species in slow exchange, Biochemistry, 28, 3383, 1989. 

Holmgren, A. (1972). Tryptophan fluorescence study of conformational transitions of the oxidized and reduced form of thioredoxin. J Biol Chem 247, 1992-8. 

DNA Y-junctions have been used as fluorescent scaffolds for EcoRII methyltransferase-thioredoxin (M EcoRII-Trx) fusion proteins and covalent links were formed between the DNA scaffold and the methyltransferase at preselected sites on the scaffold containing 5FdC [8]. The resulting... 

Data of the rate of ATP hydrolysis on the one hand, of e -flow and H/e ratio on the other hand for conditions of identical transmembrane ApH measured by fluorescence quenching AF/F of NED. ATP hydrolysis has been initiated by preillumination for 70 s in the presence of benzylviologen, thioredoxin, DTT and e -flow was induced by steady illumination in the presence of ferricyanide. The light intensity was 200 Wm-2. 

Wong, J. H. Yano, H. Lee, Y. M. Cho, M. J. Buchanan, B. B. Identiflcation of thioredoxin-linked proteins by fluorescence labeling combined with isoelectric focusing/sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Methods Enzymol 2002, 347, 339-349. 

Holmgren, A. Tryptophan Fluorescence Study of Conformational Transition of the Oxidized and Reduced Form of Thioredoxin. J. Biol. Chem. 247, 1992-1998 (1972). 

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