Output details

Near-Atomic Resolution Neutron Crystallography on PerdeuteratedPyrococcus furiosusRubredoxin: Implication of Hydronium Ions and Protonation State Equilibria in Redox Changes

Neutron diffraction has been used in conjunction with protein perdeuteration to carry out high resolution structural studies of rubredoxin in both oxidised and reduced forms. Hydronium ions are clearly identified in the structure, as well as a tautomeric shift between amino and imino forms of an amino acid residue. The results imply the importance of water-hydronium equilibria in charge transfer. The work attracted significant funding from the EU (RII3-CT-2003-505925) and the EPSRC (EP/C015452/1, GR/R47950/01) including for developments at the Institut Laue Langevin in which Forsyth was instrumental.