A reverse labelling approach to shed light on the role and presence of hydronium ions and imidic aced tautomeric effects in proteins
This is a resubmission of proposal 8-01-535 rejected on the basis of the fact that it was not obvious what the proposed experiment would add to already published data. We request beamtime on D19 for room temperature (RT) neutron crystallographic studies of perdeuterated rubredoxin in H2O, extending previous work which revealed, at 0.88A resolution, a remarkable network of ordered water that includes hydronium ions. Residue Leu51 from the RT structure of the oxidised form presents an imidic acid tautomeric equilibrium that is absent in the reduced form. It was observed that every RT oxidised rubredoxin neutron structure over the last ~15 years from various groups presents this mysterious peak. This feature appears to be of direct relevance to elucidate the implications of the redox state in the immediate vicinity of the catalytic centre. We wish to carry out a detailed crystallographic study of this network of hydroniums and tautomeric equilibrium by reverse labelling the water around the protein with H2O. The key aspect of this study is that the hydrogen atoms will appear as negative peaks in the Fourier maps and allow a clear and unambiguous visualisation of this network.
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CUYPERS Maxime; Juliette M. Devos; FORSYTH Victor Trevor; HAERTLEIN Michael; LEMEE Marie Helene; MITCHELL Edward and MOSSOU Estelle. (2019). A reverse labelling approach to shed light on the role and presence of hydronium ions and imidic aced tautomeric effects in proteins. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-01-544
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