Uncovering the relationship between the change in heat capacity for enzyme catalysis and vibrational frequency through isotope effect studies.

Jones HB, Crean RM, Matthews C, Troya A, Danson MJ, Bull SD, Arcus VL*, van der Kamp MW*, Pudney CR*. 2017. ACS Catalysis. In press


A complete thermodynamic analysis of enzyme turnover links the free energy landscape to enzyme catalysis.

Jones HB, Wells SA, Prentice EJ, Kwok A, Liang LL, Arcus VL*, Pudney CR*. 2017. FEBS J. 284, 2829


Steady-state kinetics of alpha-synuclein ferrireductase activity identifies the catalytically competent species.

Jennifer S. McDowall, Ioanna Ntai, Jonathon Hake, Paul R. Whitley, Jody M. Mason, Christopher R. Pudney* and David R Brown*. 2017. Biochemistry. 56, 2497


The red edge excitation shift phenomenon can be used to unmask protein structural ensembles: implications for NEMO-ubiquitin interactions.

Catici DA, Amos HE, Yang Y, van den Elsen JM, Pudney CR. 2016. FEBS. J. 283, 2272


Modelling flavoenzymatic charge transfer events: development of catalytic indole deuteration strategies.

Murray AT, Challinor JD, Gulácsy CE, Lujan C, Hatcher LE, Pudney CR*, Raithby PR, John MP, Carbery DR*. 2016. Org Biomol Chem. In press


On the temperature dependence of enzyme-catalyzed rates.

Vickery L. Arcus, Erica J. Prentice, Joanne K. Hobbs, Adrian J. Mulholland, Marc W. van der Kamp, Christopher Roland Pudney, Emily J. Parker, and Louis A. Schipper. 2016. Biochemistry. 55, 1681.


Change in heat capacity accuratley predicts vibrational coupling in enzyme catalysed reactions.

Arcus VL* and Pudney CR*. 2015. FEBS Lett. 589, 2200.


Poly-ubiquitin drives the molecular interactions of NF-kappaB essential modulator by allosteric regulation.

Catici DAM, Horne JE, Cooper GE, Pudney CR*. 2015. J Biol. Chem. 290, 14130.


Practical Aspects on the Use of Kinetic Isotope Effects as Probes of Flavoprotein Enzyme Mechanisms.

Pudney CR, Hay S, Scrutton NS. 2014. Methods Mol. Biol. 1146, 161.


Excited state dynamics can be used to probe donor-acceptor distances for H-tunneling reactions catalyzed by flavoproteins.

Hardman SJ, Pudney CR, Hay S, Scrutton NS. 2013. Biophys. J. 105, 2549


Enzymatic single-molecule kinetic isotope effects.

Pudney CR, Lane RS, Fielding AJ, Magennis SW, Hay S, Scrutton NS. 2013. J. Am. Chem. Soc. 135, 3855.



Fast protein motions are coupled to enzyme H-transfer reactions.

Pudney CR, Guerriero A, Baxter NJ, Johannissen LO, Waltho JP, Hay S, Scrutton NS. 2013. J. Am. Chem. Soc. 135, 2512.



Kinetic and spectroscopic probes of motions and catalysis in the cytochrome P450 reductase family of enzymes.

Pudney CR, Heyes DJ, Khara B, Hay S, Rigby SE, Scrutton NS. 2012. FEBS J. 279, 1534.



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.

Leferink NG, Pudney CR, Brenner S, Heyes DJ, Eady RR, Samar Hasnain S, Hay S, Rigby SE, Scrutton NS. 2012. FEBS Lett. 586, 578.



Coupled motions direct electrons along human microsomal P450 Chains.

Pudney CR, Khara B, Johannissen LO, Scrutton NS. 2011.PLoS Biol. 9(12):e1001222.



Probing active site geometry using high pressure and secondary isotope effects in an enzyme-catalysed 'deep' H-tunnelling reaction.

Hay S, Pudney CR, Sutcliffe MJ, Scrutton NS. 2010. J. Phys. Org. Chem. 23, 696.



Direct analysis of donor-acceptor distance and relationship to isotope effects and the force constant for barrier compression in enzymatic H-tunneling reactions.

Pudney CR, Johannissen LO, Sutcliffe MJ, Hay S, Scrutton NS. 2010. J. Am. Chem. Soc. 132, 11329.



Biocatalysis with thermostable enzymes: structure and properties of a thermophilic 'ene'-reductase related to old yellow enzyme.

Adalbjörnsson BV, Toogood HS, Fryszkowska A, Pudney CR, Jowitt TA, Leys D, Scrutton NS. 2010. Chembiochem. 11, 197.



Evidence to support the hypothesis that promoting vibrations enhance the rate of an enzyme catalyzed H-tunneling reaction.

Pudney CR, Hay S, Levy C, Pang J, Sutcliffe MJ, Leys D, Scrutton NS. 2009. J. Am. Chem. Soc. 131, 17072.



Bipartite recognition and conformational sampling mechanisms for hydride transfer from nicotinamide coenzyme to FMN in pentaerythritol tetranitrate reductase.

Pudney CR, Hay S, Scrutton NS. 2009. FEBS J. 276, 4780.



Structural and mechanistic aspects of flavoproteins: probes of hydrogen tunnelling.

Hay S, Pudney CR, Scrutton NS. 2009. FEBS J. 276, 3930.



Parallel pathways and free-energy landscapes for enzymatic hydride transfer probed by hydrostatic pressure.

Pudney CR, McGrory T, Lafite P, Pang J, Hay S, Leys D, Sutcliffe MJ, Scrutton NS. 2009. Chembiochem. 10, 1379.



Barrier compression enhances an enzymatic hydrogen-transfer reaction.

Hay S, Pudney CR, McGrory TA, Pang J, Sutcliffe MJ, Scrutton NS.2009. Angew Chem Int Ed Engl. 48, 1452.



Correction of pre-steady-state KIEs for isotopic impurities and the consequences of kinetic isotope fractionation.

Hay S, Pudney CR, Hothi P, Scrutton NS. 2008. J. Phys. Chem. A. 47, 537.



Solvent as a probe of active site motion and chemistry during the hydrogen tunnelling reaction in morphinone reductase.

Hay S, Pudney CR, Sutcliffe MJ, Scrutton NS. 2008. Chemphyschem. 19, 1875.



Atomistic insight into the origin of the temperature-dependence of kinetic isotope effects and H-tunnelling in enzyme systems is revealed through combined experimental studies and biomolecular simulation.

Hay S, Pudney C, Hothi P, Johannissen LO, Masgrau L, Pang J, Leys D, Sutcliffe MJ, Scrutton NS. 2008. Biochem. Soc. Trans. 36, 16.



Are environmentally coupled enzymatic hydrogen tunneling reactions influenced by changes in solution viscosity?

Hay S, Pudney CR, Sutcliffe MJ, Scrutton NS. 2008. Angew Chem Int Ed Engl. 47, 537.



Mutagenesis of morphinone reductase induces multiple reactive configurations and identifies potential ambiguity in kinetic analysis of enzyme tunneling mechanisms.

Pudney CR, Hay S, Pang J, Costello C, Leys D, Sutcliffe MJ, Scrutton NS. 2007. J. Am. Chem. Soc. 129, 13949.



Alpha-secondary isotope effects as probes of "tunneling-ready" configurations in enzymatic H-tunneling: insight from environmentally coupled tunneling models.

Pudney CR, Hay S, Sutcliffe MJ, Scrutton NS. 2006. J. Am. Chem. Soc. 128, 14053.