Fluorescence and Excitation Escherichia Coli RecA Protein Spectra Analyzed Separately for Tyrosine and Tryptophan Residues

Fluorescence quenching in the DsbA prote

Fluorescence quenching in the DsbA protein from Escherichia coli: Complete picture of the excited-state energy pathway and evidence for the reshuffling dynamics of the microstates of tryptophan

✍ Alain Sillen; Jens Hennecke; Daniela Roethlisberger; Rudi Glockshuber; Yves Enge 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 253 KB 👁 2 views

The disulfide oxidoreductase DsbA is a strong oxidant of protein thiols and is required for efficient disulfide bond formation in the bacterial periplasm. DsbA contains two tryptophans: W76 and W126. The fluorescence of W76 changes upon reduction of the disulfide bridge, as analyzed previously (Henn