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Catici, D. A. M., Amos, H. E., Yang, Y., van den Elsen, J. M. H. and Pudney, C. R., 2016. The red edge excitation shift phenomenon can be used to unmask protein structural ensembles:implications for NEMO-ubiquitin interactions. FEBS Journal, 283 (12), pp. 2272-2284. Murray, A. T., Challinor, J. D., Gulácsy, C. E., Lujan, C., Hatcher, L. E., Pudney, C. R., Raithby, P. R., John, M. P. and Carbery, D. R., 2016. Modelling flavoenzymatic charge transfer events:development of catalytic indole deuteration strategies. Organic and Biomolecular Chemistry, 14 (15), pp. 3787-3792. Arcus, V. L., Prentice, E. J., Hobbs, J. K., Mulholland, A. J., van der Kamp, M. W., Pudney, C. R., Parker, E. J. and Schipper, L. A., 2016. On the temperature dependence of enzyme-catalyzed rates. Biochemistry, 55 (12), pp. 1681-1688. Pudney, Christopher, 2016. Measuring protein flexibility and conformational state. 1604640.1, 2016. Arcus, V. L. and Pudney, C. R., 2015. Change in heat capacity accurately predicts vibrational coupling in enzyme catalyzed reactions. FEBS Letters, 589 (17), pp. 2200-2206. Catici, D. A. M., Horne, J. E., Cooper, G. E. and Pudney, C. R., 2015. Poly-ubiquitin drives the molecular interactions of NF-κB essential modulator (NEMO) by allosteric regulation. Journal of Biological Chemistry, 290 (22), pp. 14130-14139. Pudney, C. R., Hay, S. and Scrutton, N. S., 2014. Practical aspects on the use of kinetic isotope effects as probes of flavoprotein enzyme mechanisms. In: Weber, S. and Schleicher, E., eds. Flavins and Flavoproteins. New York: Humana Press, pp. 161-175. Hardman, S., Pudney, C. R., Hay, S. and Scrutton, N. S., 2013. Excited state dynamics can be used to probe donor-acceptor distances for H-tunneling reactions catalysed by flavoproteins. Biophysical Journal, 105 (11), pp. 2549-2558. Pudney, C. R., Lane, R. S. K., Fielding, A. J., Maggenis, S. W., Hay, S. and Scrutton, N. S., 2013. Enzymatic single-molecule kinetic isotope effects. Journal of the American Chemical Society, 135 (10), pp. 3855-3864. Pudney, C., Guerriero, A., Baxter, N. J., Johannissen, L. O., Waltho, J. P., Hay, S. and Scrutton, N. S., 2013. Fast protein motions are coupled to enzyme H-transfer reactions. Journal of the American Chemical Society, 135 (7), pp. 2512-2517. Pudney, C., Heyes, D. J., Khara, B., Hay, S., Rigby, S. E. J. and Scrutton, N. S., 2012. Kinetic and spectroscopic probes of motions and catalysis in the cytochrome P450 Reductase family of enzymes. FEBS Journal, 279 (9), pp. 1534-1544. Leferink, N. G. H., Pudney, C., Brenner, S., Heyes, D. J., Eady, R. R., Hasnain, S. S., Hay, S., Rigby, S. E. J. and Scrutton, N. S., 2012. Gating mechanisms for biological electron transfer: Integrating structure with biophysics reveals the nature of redox control in cytochrome P450 reductase and copper-dependent nitrite reductase. FEBS Letters, 586 (5), pp. 578-584. Pudney, C. R., Khara, B., Johannissen, L. O. and Scrutton, N. S., 2011. Coupled motions direct electrons along human microsomal P450 chains. PLoS Biology, 9 (12), e1001222. Hay, S., Pudney, C., Sutcliffe, M. J. and Scrutton, N. S., 2010. Probing active site geometry using high pressure and secondary isotope effects in an enzyme-catalysed ‘deep’ H-tunneling reaction. Journal of Physical Organic Chemistry, 23 (7), pp. 696-701. Adalbjornson, B., Fryszkowska, A., Toogood, H., Pudney, C., Jowitt, T. A., Leys, D. and Scrutton, N. S., 2010. Biocatalysis with thermostable enzymes: Structure and properties of a thermophilic “ene”-reductase related to Old Yellow Enzyme. ChemBiochem, 11 (2), pp. 197-207. Pudney, C., Johannissen, L. O., Sutcliffe, M. J., Hay, S. and Scrutton, N. S., 2010. Direct analysis of donor-acceptor distance and relationship to isotope effects and the force constant for barrier compression in enzymatic H-tunneling reactions. Journal of the American Chemical Society, 132 (32), pp. 11329-11335. Pudney, C., Hay, S. and Scrutton, N. S., 2009. Bipartite recognition and conformational sampling mechanisms for hydride transfer from nicotinamide coenzyme to FMN in pentaerythritol tetranitrate reductase. FEBS Journal, 276 (17), pp. 4780-4789. Hay, S., Pudney, C. and Scrutton, N. S., 2009. Structural and mechanistic aspects of flavoproteins: Probes of hydrogen tunneling. FEBS Journal, 276 (15), pp. 3930-3941. Pudney, C., McGrory, T., Lafite, P., Pang, J., Hay, S., Leys, D., Sutcliffe, M. J. and Scrutton, N. S., 2009. Parallel pathways and free-energy landscapes for enzymatic hydride transfer probed by hydrostatic pressure. ChemBiochem, 10 (8), pp. 1379-1384. Hay, S., Pudney, C., McGrory, T. A., Pang, J., Sutcliffe, M. J. and Scrutton, N. S., 2009. Barrier compression enhances an enzymatic hydrogen-transfer reaction. Angewandte Chemie-International Edition, 121 (8), pp. 1480-1483.