High resolution monochromatic neutron diffraction study of the Fe-reduced form of perdeuterated rubredoxin
We request beamtime on D19 for a full structural study of reduced-Fe (i.e. Fe2+) perdeuterated rubredoxin. This proposal follows outstanding results obtained from D19 experiment 1-20-16 on the oxidised (Fe3+) form, which provided data with high completeness to a resolution of 1.19Å. This is the one of the highest resolutions ever described for a neutron crystallographic study of any protein, and has resulted in some remarkable observations. Of particular note is the occurrence of a perdeuterated hydronium ion as well as evidence of tautomeric equilibrium between neighbouring amino acid residues. These observations were only possible through the use of high resolution neutron crystallography, and the study is currently being prepared for publication. In this proposal we seek to extend this work by carrying out a comparable study of the Fe2+ form of the same protein. This is likely to provide crucial information that may be of central importance for an understanding of the redox mechanism linking the two forms, and the role that protonation shifts may play in them.
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CUYPERS Maxime; FORSYTH Victor Trevor; MASON, Sax A. and MITCHELL Edward. (2012). High resolution monochromatic neutron diffraction study of the Fe-reduced form of perdeuterated rubredoxin. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-01-389
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