Neutron scattering studies of dynamics and proton tunneling in a redox protein.
Rubredoxins are small monomeric iron-sulphur cluster proteins that act as electron carriers in a variety of biological activities. High-resolution neutron and X-ray crystal structures of Rubredoxin from Pyrococcus furiosus (Pf), an extremely thermostable protein, have highlighted a structured network of water, hydronium ions and Zundel ions linking to its iron-sulphur center. This suggests that protonation shifts involving exotic ionic species might be involved in the charge transfer processes of redox proteins. Using the IN16b backscattering beamline, we aim to: (1) use neutron scattering to investigate the possibility of tunneling phenomena in this Pf rubredoxin protein where it seems highly likely that proton shifts through a structured molecular network may form a crucial part of the redox activity of the system, by recording a full spectrum at very low temperature; (2) study the temperature-dependent dynamics of the Pf Rubredoxin and see how it compares to that of other previously-studied proteins. To this effect, we propose to carry out elastic and inelastic fixed-window measurements on the same hydrogenated powder sample of Pf rubredoxin.
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Juliette M. Devos; CUYPERS Maxime; FORSYTH Victor Trevor; GLYDE Henry; HAERTLEIN Michael; JIMENEZ RUIZ Monica; MOSSOU Estelle and SEYDEL Tilo. (2019). Neutron scattering studies of dynamics and proton tunneling in a redox protein.. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-850
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