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Near-Atomic Resolution Neutron Crystallography on Perdeuterated Pyrococcus furiosus Rubredoxin: Implication of Hydronium Ions and Protonation State Equilibria in Redox Changes

Authors


  • V.T.F. and S.A.M. acknowledge EPSRC support for the construction of the D19 diffractometer under grant GR/R47950/01 to Durham, Keele, and Bath Universities. V.T.F. also acknowledges EPSRC support under grant EP/C015452/1 and from the EU under contract RII3-CT-2003-505925. We thank the ILL for provision of neutron beamtime on D19, and the ESRF for time on beamline ID-29. We gratefully acknowledge J. B. Artero and M. Moulin for help with fermentation procedures.

Abstract

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Neutron crystallographic analyses at near-atomic resolution are presented for both reduced and oxidized forms of perdeuterated Pyrococcus furiosus rubredoxin, a small iron–sulfur redox protein with remarkable thermostability. Hydronium ions may play a key role in the protonation and charge-transfer processes associated with the oxidized and reduced forms of the protein. Picture: overall structure showing D3O+ ions (red and gray molecules).

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