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

Podobne zapisy

• Evidence for a Novel Mechanism of Time-Resolved Flavin Fluorescence Depolarization in Glutathione Reductase
  od: van den Berg, Petra A. W., i wsp.
  Wydane: (2004)
• Flavin fluorescence dynamics and photoinduced electron transfer in Escherichia coli glutathione reductase.
  od: van den Berg, P A, i wsp.
  Wydane: (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.
  od: Mulrooney, S. B., i wsp.
  Wydane: (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.
  od: Veine, D. M., i wsp.
  Wydane: (1998)
• Equilibrium and ultrafast kinetic studies manipulating electron transfer: A short-lived flavin semiquinone is not sufficient for electron bifurcation
  od: Hoben, John P., i wsp.
  Wydane: (2017)