Exploring the conformational equilibrium of E. coli thioredoxin reductase: Characterization of two catalytically important states by ultrafast flavin fluorescence spectroscopy

Samankaltaisia teoksia

• Evidence for a Novel Mechanism of Time-Resolved Flavin Fluorescence Depolarization in Glutathione Reductase
  Tekijä: van den Berg, Petra A. W., et al.
  Julkaistu: (2004)
• Flavin fluorescence dynamics and photoinduced electron transfer in Escherichia coli glutathione reductase.
  Tekijä: van den Berg, P A, et al.
  Julkaistu: (1998)
• Evidence for two conformational states of thioredoxin reductase from Escherichia coli: use of intrinsic and extrinsic quenchers of flavin fluorescence as probes to observe domain rotation.
  Tekijä: Mulrooney, S. B., et al.
  Julkaistu: (1997)
• 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.
  Tekijä: Veine, D. M., et al.
  Julkaistu: (1998)
• Hydrogen Bond Switching among Flavin and Amino Acid Side Chains in the BLUF Photoreceptor Observed by Ultrafast Infrared Spectroscopy
  Tekijä: Bonetti, Cosimo, et al.
  Julkaistu: (2008)