2005 - 2009 Publications

[254] Structure-based mechanism of CMP-Kdo synthetase: convergent evolution of a sugar activating enzyme with DNA-/RNA-polymerases (2009)

Heyes, D. J., Levy, C., Lafite, P., Roberts, I. S., Goldrick, M., Stachulski, A. V., Rossington, S., Stanford, D., Rigby, S. E. J., Scrutton, N. S. & Leys, D.

Journal of Biological Chemistry, 284, 35514-35523, DOI: 10.1074/jbc.M109.056630 Free Access

[253] Continuous wave photolysis magnetic field effect investigations with free and protein-bound alkylcobalamins: the role of radical quenching (2009)

Jones, A. R., Woodward, J. R. & Scrutton, N. S.,

Journal of the American Chemical Society, 131, 17246-17253, DOI: 10.1021/ja9059238

[252] Evidence to support the hypothesis that promoting vibrations enhance the rate of an enzyme catalyzed H-tunneling reaction (2009)

Pudney, C. R., Hay, S., Levy, C., Pang, J., Sutcliffe, M. J., Leys, D. & Scrutton, N. S.

Journal of the American Chemical Society, 131, 17072-17073, DOI: 10.1021/ja908469m

[251] Asymmetric reduction of activated alkenes by pentaerythritol tetranitrate reductase: specificity and control of stereochemical outcome by reaction optimisation (2009)

Fryszkowska, A., Toogood, H., Sakuma, M., Gardiner, J. M., Stephens, G. M. & Scrutton, N. S.

Advanced Synthesis & Catalysis, 351, 2976-2990, DOI: 10.1002/adsc.200900574

[250] Are the catalytic properties of enzymes from piezophilic organisms pressure adapted? (2009)

Hay, S., Evans, R. M., Levy, C., Loveridge, E. J., Wang, X., Leys, D., Allemann, R. K. & Scrutton N. S.

ChemBioChem., 10, 2348-2353, DOI: 10.1002/cbic.200900367

[249] Demonstration of proton coupled electron transfer in the copper containing enzyme nitrite reductase (2009)

Brenner, S., Heyes, D. J., Hay, S., Hough, M. A., Eady, R. R., Hasnain, S. S. & Scrutton N. S.

Journal of Biological Chemistry., 284, 25973-25983, DOI: 10.1074/jbc.M109.012245 Free Access

[248] Bipartite recognition and conformational sampling mechanisms for hydride transfer from nicotinamide coenzyme to FMN in pentaerythritol tetranitrate reductase. (2009)

Pudney, C. R., Hay, S. & Scrutton N. S.

FEBS Journal, 276, 4780-4789, DOI: 10.1111/j.1742-4658.2009.07179.x Free Access

[247] Structural and mechanistic aspects of flavoproteins: probes of hydrogen tunneling (2009)

Hay S, Pudney, C. R. & Scrutton, N. S.

FEBS Journal, 276, 3930-3941, DOI: 10.1111/j.1742-4658.2009.07121.x Free Access

[246] Probing the molecular determinants of coenzyme selectivity in the P450 BM3 FAD/NADPH domain (2009)

Dunford, A.J., Girvan, H., M., Scrutton N. S. & Munro A. W.,

Biochim. Biophys. Acta, 1794, 1181-1189, DOI: 10.1016/j.bbapap.2009.03.014

[245] Cryogenic and laser photoexcitation studies identify multiple roles for active site residues in the light-driven enzyme protochlorophyllide oxidoreductase (2009)

Menon, B., Waltho, J. P., Scrutton, N. S. & Heyes, D. J.

Journal of Biological Chemistry, 284, 18160-18166, DOI: 10.1074/jbc.M109.020719 Free Access

[244] What's in a covalent bond? On the role and formation of covalently bound flavin cofactors (2009)

Heuts, D. P. H. M., Scrutton, N. S., McIntire, W. S. & Fraaije, M. W.

FEBS Journal, 276, 3405-3427, DOI: 10.1111/j.1742-4658.2009.07053.x Free Access

[243] An internal reaction chamber in dimethylglycine oxidase provides efficient protection from exposure to toxic formaldehyde (2009)

Tralau, T., Lafite, P., Levy, C., Combe, J. P., Scrutton N. S. & Leys, D.

Journal of Biological Chemistry., 284, 17826-17834, DOI: 10.1074/jbc.M109.006262 Free Access

[242] Parallel pathways and free energy landscapes for enzymatic hydride transfer probed by hydrostatic pressure (2009)

Pudney, C. R., McGrory, T., Lafite, P., Pang, J., Hay, S., Leys, D., Sutcliffe, M. J. & Scrutton, N. S.

ChemBioChem., 10, 1379-1384, DOI: 10.1002/cbic.200900071

[241] Cobalamin uptake and reactivation occurs through specific protein interactions in the methionine synthase-methionine synthase reductase complex ( 2009)

Wolthers, K. R., & Scrutton, N. S.

FEBS Journal, 276, 1942-1951, DOI: 10.1111/j.1742-4658.2009.06919.x, Free Access Faculty 1000 recommended

[240] Time resolved studies of radical pairs (2009)

Woodward, J. R., Foster, T. J., Jones, A. R., Salaoru, A. T. & Scrutton, N. S.

Biochemical Society Transactions 37, 358-362, DOI: 10.1042/BST0370358

[239] Conformational changes in the catalytic cycle of protochlorophyllide oxidoreductase: what lessons can be learnt from dihydrofolate reductase? (2009)

Heyes, D. J. & Scrutton, N. S.

Biochemical Society Transactions. 37, 354-357, DOI: 10.1042/BST0370354

[238] Enzyme mechanisms: fast reaction and computational approaches (2009). Munro, A. W. & Scrutton, N. S. Biochemical Society Transactions. 37, 333-335, DOI: 10.1042/BST0370333

[237] Solvent slaved protein motions accompany proton but not hydride tunneling in light-activated protochlorophyllide oxidoreductase (2009)

Heyes, D. J., Sakuma, M., & Scrutton, N. S.,

Angewandte Chemie Int. Ed., 48, 3850 – 3854, DOI: 10.1002/ange.200900086

[236] Computational simulations of tunnelling reactions in enzymes (2009)

Pang, J., Scrutton, N. S. & Sutcliffe, M. J.

‘Quantum tunnelling in enzyme catalysed reactions’ RSC Biomolecular Sciences Series (Eds Allemann, R. K. & Scrutton, N. S.), Royal Society of Chemistry Publishing. pp. 219-241

[235] Probing coupled motions in enzymatic hydrogen tunnelling reactions: beyond temperature-dependence studies of kinetic isotope effects (2009)

Hay, S., Sutcliffe, M. J. & Scrutton, N. S.

‘Quantum tunnelling in enzyme catalysed reactions’ RSC Biomolecular Sciences Series (eds Allemann, R. K. & Scrutton, N. S.), Royal Society of Chemistry Publishing. pp. 242-267

[234] Nuclear quantum tunneling in the light-activated enzyme protochlorophyllide oxidoreductase (2009)

Heyes, D. J., Sakuma, M., De Visser, S. & Scrutton, N. S.

Journal of Biological Chemistry. 284, 3762-3767, DOI: 10.1074/jbc.M808548200, Free Access Editors’ Choice (2009) Science 323, 562. Faculty 1000 recommended.

[233] Internal electron transfer in multi-site redox enzymes is accessed by laser excitation of thiouredopyrene-3,6,8-trisulfonate (TUPS) (2009)

Heyes, D. J., Quinn, A. M., Cullis P.M., Lee, M., Munro, A. W. & Scrutton, N. S.

Chem. Comm. 9, 1124-1126, DOI: 10.1039/B820386E

[232] Characterisation of coenzyme binding and selectivity determinants in Mycobacterium tuberculosis FprA: analysis of Arg199 and Arg200 mutants at the NADP(H) 2’-phosphate binding site (2009)

Sabri, M., Dunford, A. J., McLean, K. J., Neeli, R., Scrutton, N. S., Leys, D. & Munro A. W.,

Biochemical Journal, 417,103-112, DOI: 10.1042/BJ20080466

[231] Barrier compression enhances an enzymatic H-transfer reaction (2009)

Hay, S., Pudney, C. R., McGrory, T., Pang, J., Sutcliffe, M. J. & Scrutton, N. S.,

Angewandte Chemie International Ed., 48, 1452-1454, DOI: 10.1002/ange.200805502

[230] Correction of pre-steady-state KIEs for isotopic impurities and the consequences of kinetic isotope fractionation (2008)

Hay, S., Pudney, C. R., Hothi, P. & Scrutton, N. S.

Journal of Physical Chemistry A., 112, 13109-13115, DOI: 10.1021/jp805107n

[229] Mechanism of radical based catalysis in the reaction catalysed by ornithine 4,5 aminomutase (2008)

Wolthers, K. R., Rigby, S. E. J. & Scrutton, N. S.

Journal of Biological Chemistry., 283, 34615-34625, DOI: 10.1074/jbc.M807911200 Free Access

[228] The enzyme aromatic amine dehydrogenase induces a substrate conformation crucial for a promoting vibration that significantly reduces the effective potential energy barrier to proton transfer (2008)

Johannissen, L., Scrutton, N. S. & Sutcliffe, M. J.

Journal of the Royal Society. Interface, 3, S225-232

[227] Reduction of aliphatic nitroesters and N-nitramines by Enterobacter cloacae PB2 pentaerythritol tetranitrate reductase: quantitative structure-activity relationships (2008)

Nivinskas, H., Sarlauskas, J., Anusevicius, Z., Toogood, H. S., Scrutton, N. S. & Cenas, N.

FEBS Journal, 275, 6192 - 6203, DOI: 10.1111/j.1742-4658.2008.06744.x Free Access

[226] Driving force analysis of proton tunnelling across a reactivity series for an enzyme-substrate complex (2008)

Hothi, P., Hay, S., Roujeinikova, A., Sutcliffe, M. J., Lee, M., Leys, D., Cullis, P. M. & Scrutton, N. S.

ChemBioChem., 9, 2839-2845, DOI: 10.1002/cbic.200800408

[225] Structure-based insight into the asymmetric bioreduction of the C=C double bond of a,b-unsaturated nitroalkenes by pentaerythritol tetranitrate reductase (2008)

Toogood, H. S., Fryszkowska, A., Hare, V., Fisher, K., Roujeinikova, A., Leys, D., Gardiner, J. M., Stephens, G. M. & Scrutton, N. S.

Advanced Synthesis & Catalysis, 350, 2789-2803, DOI: 10.1002/adsc.200800561

[224] Conformational events during ternary enzyme-substrate complex formation are rate limiting in the catalytic cycle of the light-driven enzyme protochlorophyllide oxidoreductase (2008)

Heyes, D. J., Menon, B. R. K., Sakuma, M. & Scrutton, N. S.

Biochemistry 47, 10991-10998, DOI: 10.1021/bi801521c

[223] H-transfers in photosystem II: what can we learn from recent lessons from the enzyme community (2008)

Hay, S. & Scrutton N. S.

Photosynthesis Research, 98, 169-177, DOI: 10.1007/s11120-008-9326-x

[222] Incorporation of hydrostatic pressure into models of hydrogen tunneling highlights a role for pressure-modulated promoting vibrations (2008)

Hay, S. & Scrutton, N. S.

Biochemistry, 47, 9880-9887, DOI: 10.1021/bi8005972

[221] Solvent as a probe of active site motion and chemistry during the hydrogen tunneling reaction in morphinone reductase (2008)

Hay, S., Pudney, C. R., Sutcliffe, M. J. & Scrutton, N. S.

ChemPhysChem., 9, 1875-1881, DOI: 10.1002/cphc.200800303

[220] Interflavin electron transfer in human cytochrome P450 reductase: effects of solvent and pH identify hidden complexity in mechanism (2008). Brenner, S., Hay, S., Munro, A. W. & Scrutton, N. S., FEBS J, 275, 4540-4557 , DOI: 10.1111/j.1742-4658.2008.06597.x Free Access

[ 219] Secondary kinetic isotope effects as probes of environmentally-coupled enzymatic hydrogen tunnelling reactions (2008)

Hay, S., Pang, J., Monaghan, P. J., Wang, X., Evans, R. M., Sutcliffe, M. J., Allemann, R. K. & Scrutton, N. S.

ChemPhysChem., 9, 1536-1539, DOI: 10.1002/cphc.200800291

[218] The pH dependence of kinetic isotope effects in monoamine oxidase A indicates stabilisation of the neutral amine in the enzyme-substrate complex (2008)

Dunn, R. V., Marshall K., Munro, A. W. & Scrutton, N. S.

FEBS Journal, 275, 3850-3858, DOI: 10.1111/j.1742-4658.2008.06532.x Free Access

[217] Deep tunneling dominates the biologically important hydride transfer reaction from NADH to FMN in morphinone reductase (2008)

Pang, J., Hay, S., Scrutton, N. S. & Sutcliffe, M. J.

Journal of the American Chemical Society, 130, 7092-7097, DOI: 10.1021/ja800471f

[216] Probing the dynamic interface between trimethylamine dehydrogenase (TMADH) and electron transferring flavoprotein (ETF) in the TMADH—2ETF complex: role of the Arg-a237 (ETF) and Tyr-442 (TMADH) residue pair (2008)

Burgess, S. G., Messiha, H. L., Katona, G., Rigby, S. E. J., Leys, D. & Scrutton, N. S.

Biochemistry, 47, 5168-5181, DOI: 10.1021/bi800127d

[215] Robotic high-throughput screening of pentaerythritol tetranitrate reductase mutants for the generation of useful biocatalysts (2008)

Toogood, H., Hulley, M., Heyes, D. J., Fryszkowska, A., Fisher, K., Stephens, G. M. & Scrutton, N. S.

Flavins and Flavoproteins ; Proceedings of the sixteenth International Symposium. Jaca, Spain (Eds. Frago, S, Gomez-Moreno, C & Medina, M.) Prensas Universitarias de Zaragoza, Spain pp. 543-546

[214] Characterisation of AIFM2: a novel human apoptosis inducing flavoprotein (2008)

Collins, H. F., Mclean, K. J., Tang, C. W., Jackson, D. A., Scrutton, N. S. & Munro, A. W.

Flavins and Flavoproteins ; Proceedings of the sixteenth International Symposium. Jaca, Spain (Eds. Frago, S, Gomez-Moreno, C & Medina, M.) Prensas Universitarias de Zaragoza, Spain pp. 285-290

[213] Reduction of diflavin enzymes by photoexcitable thiouredopyrene-3,6,8-trisulfonate (TUPS) (2008)

Heyes, D. J., Quinn, A. M., Cullis, P., Lee, M., Munro, A. W. & Scrutton, N. S.

Flavins and Flavoproteins ; Proceedings of the sixteenth International Symposium. Jaca, Spain (Eds. Frago, S, Gomez-Moreno, C & Medina, M.) Prensas Universitarias de Zaragoza, Spain pp. 315-320

[212] Promoting motions facilitate nuclear tunneling in flavoprotein enzymes (2008)

Hay, S., Pudney, C. R., Pang, J., Leys, D., Sutcliffe, M. J. & Scrutton, N. S.

Flavins and Flavoproteins ; Proceedings of the sixteenth International Symposium. Jaca, Spain (Eds. Frago, S, Gomez-Moreno, C & Medina, M.) Prensas Universitarias de Zaragoza, Spain pp. 415-426

[211] pH dependence of monoamine oxidase A activity (2008)

Dunn, R. V., Munro, A. W. & Scrutton, N. S.

Flavins and Flavoproteins; Proceedings of the sixteenth International Symposium. Jaca, Spain (Eds. Frago, S, Gomez-Moreno, C & Medina, M.) Prensas Universitarias de Zaragoza, Spain, pp. 187-192

[210] Tryptophan 359 regulates flavin thermodynamics and coenzyme selectivity in Mycobacterium tuberculosis Fpr A (2008)

Neeli, R., Sabri, M., Mclean, K. J., Dunford, A. J., Scrutton, N. S., Leys, D. & Munro, A. W.

Biochemical Journal, 411, 563-570, DOI: 10.1042/BJ20071298

[209] 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 (2008)

Hay, S., Pudney, C., Hothi, P., Johannissen, L. O., Masgrau, L., Pang, J., Leys, D., Sutcliffe, M. J. & Scrutton, N. S.

Biochemical Society Transactions, 36, 16-21, DOI: 10.1042/BST0360016

[208] Catalysis by the isolated tryptophan tryptophylquinone (TTQ)-containing subunit of aromatic amine dehydrogenase is distinct from native enzyme and synthetic model compounds and allows further probing of TTQ mechanism. (2008)

Hothi, P., Lee, M., Cullis, P. M., Leys, D. & Scrutton, N. S.

Biochemistry, 47, 183-194, DOI: 10.1021/bi701690u

[207] Evidence for protein conformational change at a Au(110)/protein interface (2008)

Messiha, H. L., Smith, C. I., Scrutton, N. S. & Weightman, P.

Eur. Phys. Letts 83, 18004, DOI: 10.1209/0295-5075/83/18004

[206] Are environmentally coupled enzymatic hydrogen tunnelling reactions influenced by changes in solution viscosity? (2008)

Hay, S., Pudney, C.R., Sutcliffe, M. J. & Scrutton, N. S.

Angewandte Chemie International Ed., 47, 537-540, DOI: 10.1002/anie.200704484

[205] Magnetic field effect studies indicate the radical pair in adenosylcobalamin-dependent ethanolamine ammonia lyase is stabilized against geminate recombination (2007)

Jones, A., Hay, S., Woodward, J. R. & Scrutton, N. S.

Journal of the American Chemical Society, 129, 15718-15727, DOI: 10.1021/ja077124x

[204] Mutagenesis of morphinone reductase induces multiple reactive configurations and identifies a potential ambiguity in kinetic analysis of enzyme tunneling mechanisms (2007)

Pudney, C., Hay, S., Pang, J., Costello, C., Leys, D., Sutcliffe, M. J. & Scrutton, N. S.

Journal of the American Chemical Society, 129, 13949-1395, DOI: 10.1021/ja074463h

[203] Laser excitation studies of the product release steps in the catalytic cycle of the light-driven enzyme protochlorophyllide oxidoreductase (2007)

Heyes, D. J., Sakuma, M. & Scrutton, N. S.

Journal of Biological Chemistry., 282, 32015-32020,DOI: 10.1074/jbc.M706098200 Free Access

[202] Dynamics driving function: new insights from electron transferring flavoproteins and partner complexes (2007)

Toogood, H. S., Leys, D. & Scrutton, N. S.

FEBS Journal, 274, 5481-5504, DOI: 10.1111/j.1742-4658.2007.06107.x Free Access

[201] Mechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetry (2007)

Wolthers, K.R., Lou, X., Toogood, H., Leys, D. & Scrutton, N. S.

Biochemistry, 46, 11833-11844 , DOI: 10.1021/bi701209p

[200] DNA binding suppresses human AIF-M2 activity and provides a connection between redox chemistry, reactive oxygen species and apoptosis (2007)

Gong, M., Hay, S., Marshall, K. R., Munro, A. W. & Scrutton, N. S.

Journal of Biological Chemistry., 282, 30331-30340, DOI: 10.1074/jbc.M703713200 Free Access

[199] Rapid P450 heme iron reduction by laser photoexcitation of Mycobacterium tuberculosis CYP121 and CYP51B1: Analysis of CO complexation reactions and reversibility of the P450/P420 equilibrium (2007)

Dunford, A. J., McLean, K. J., Sabri, M., Seward, H. E., Heyes, D.J., Scrutton, N. S. & Munro, A. W.

Journal of Biological Chemistry., 282, 24816-24824, DOI: 10.1074/jbc.M702958200 Free Access

[198] Analysis of classical and quantum paths for deprotonation of methylamine by methylamine dehydrogenase (2007)

Ranaghan, K. E., Masgrau, L., Scrutton, N. S., Sutcliffe, M. J. & Mulholland, A. J.

ChemPhysChem., 8, 1816-1835, DOI: 10.1002/cphc.200700143

[197] New insights into the reductive half-reaction mechanism of aromatic dehydrogenase revealed by reaction with carbinolamine substrates (2007)

Roujeinikova, A., Hothi, P., Masgrau, L., Sutcliffe, M. J., Scrutton, N. S. & Leys, D.

Journal of Biological Chemistry, 282, 23766-23777, DOI: 10.1074/jbc.M700677200 Free Access

[196] Isotope effects reveal that para-substituted benzylamines are poor reactivity probes of quinoprotein mechanism in aromatic amine dehydrogenase (2007)

Hothi, P., Roujeinikova, A., Abu Khadra, K., Lee, M., Cullis, P. M., Leys, D. & Scrutton, N. S.

Biochemistry, 46, 9250-9259, DOI: 10.1021/bi7007239

[195] Conformational dynamics of the cytochrome P450 BM3/N-palmitoylglycine complex: the proposed ‘proximal-distal’ transition probed by temperature-jump spectroscopy (2007)

Brenner, S., Hay, S., Girvan, H., Munro, A. W. & Scrutton, N. S.,

Journal of Physical Chemistry B., 111, 7879-7886, DOI: 10.1021/jp073036n

[194] Protein interactions in the human methionine synthase—methionine synthase reductase complex and implications for the mechanism of enzyme reactivation (2007)

Wolthers, K. R. & Scrutton, N. S.

Biochemistry 46, 6696-6709 , DOI: 10.1021/bi700339v

[193] Laser photoexcitation of NAD(P)H induces reduction of P450 BM3 heme domain in the microsecond time domain (2007)

Girvan, H.M., Heyes, D.J., Scrutton, N.S. & Munro, A.W.

Journal of the American Chemical Society 129, 6647-6653, DOI: 10.1021/ja071355m

[192] Conformational and Thermodynamic Control of Electron Transfer in Neuronal Nitric Oxide Synthase (2007)

Dunford,A. J., Rigby,S. E. J., Hay, S., Munro,A. W., Scrutton, N. S.

Biochemistry, 46, 5018-5029, DOI: 10.1021/bi7001339 Open Access

[191] Mechanistic aspects and redox properties of hyperthermophilic L-proline dehydrogenase from Pyrococcus furiosus related to dimethylglycine dehydrogenase/oxidase (2007)

Monaghan, P. J., Leys, D. & Scrutton, N. S.

FEBS Journal, 274, 2070-2087, DOI: 10.1111/j.1742-4658.2007.05750.x Free Access

[190] Tunneling and classical paths for proton transfer in an enzyme reaction dominated by tunneling: oxidation of tryptamine by aromatic amine dehydrogenase (2007)

Masgrau, L., Ranaghan, K. E., Scrutton, N. S., Mulholland, A. J. & Sutcliffe, M. J.

Journal of Physical Chemistry B., 111, 3032-3047, DOI: 10.1021/jp067898k

[189] Proton Tunneling in Aromatic Amine Dehydrogenase is Driven by a Short-Range Sub-Picosecond Promoting Vibration: Consistency of Simulation and Theory with Experiment (2007)

Johannissen, L. O., Hay, S., Scrutton, N. S. & Sutcliffe, M. J.,

Journal of Physical Chemistry B., 111, 2631-2638, DOI: 10.1021/jp066276w

[188] Catalytic mechanism of hydride transfer between NADP+/H and ferredoxin NADP+-reductase from Anabaena PCC 7119 (2007)

Tejero, J., Peregrina, J. R., Martínez-Júlvez, M., Gutierrez, A., Gomez-Moreno, C., Scrutton, N. S. & Medina, M.

Archives of Biochemistry and Biophysics, 459, 79-90, DOI: 10.1016/j.abb.2006.10.023

[187] Crystal structure and solution characterization of the activation domain of human methionine synthase (2007)

Wolthers, K., Toogood, H., Jowitt, T., Marshall, K. R., Leys, D. & Scrutton, N. S.

FEBS Journal, 274, 738-750, DOI: 10.1111/j.1742-4658.2006.05618.x Free Access

[186] Promoting motions in enzyme catalysis probed by pressure studies of kinetic isotope effects (2007)

Hay, S., Sutcliffe, M. J. & Scrutton, N. S.,

Proc. Natl. Acad. Sci. USA, 104, 507-512, DOI: 10.1073/pnas.0608408104

[185] Two electron reduction of quinones by Enterobacter cloacae PB2 pentaerythritol tetranitrate reductase: quantitative structure-activity relationships (2007)

Miseviciene, L., Anusevicius, A., Sarlauskas, J., Harris, R. J., Scrutton, N. S. & Cenas, N.

Acta Chimica Polonica, 54, 379-385, DOI: 10.1016/S0003-9861(02)00228-X

[184] Probing of small molecules and proteins low frequency vibrations using Terahertz radiation at SRS Daresbury laboratory (2007)

Fersi, H., Gardner, P., Surman, M., Scrutton, N., Scutliffe, M.

Infrared and Millimeter Waves, and the 15th International Conference on Terahertz Electronics. IRMMW-THz. IEEE, New York, pp.393,394, DOI: 10.1109/ICIMW.2007.4516548

[183] Reduction of nitroaromatic explosives by oxygen-insensitive NAD(P)H:nitroreductases: implications for their cytotoxicity and biodegradation (2006)

Sarlauskas, J., Miseviciene, L., Nivinskas, H., Anusevicius, Z., Nemeikaite-Ceniene, A., Maldutis, E., Harris, R.J., Scrutton, N. S. & Cenas, N.

Cent. Eur. J. Energ. Mat. Vol 3, No4., 89-101

[182] Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase (2006)

Roujeinikova, A., Scrutton, N. S. & Leys, D.

Journal of Biological Chemistry, 281, 40264-40272, DOI: 10.1074/jbc.M605559200 Free Access

[181] Flavocytochrome P450 BM3 and the origin of CYP102 fusion species. (2006)

Girvan, H.M., Walthan, T.M., Neeli, R., Collins, H.F., McLean, K.J., Scrutton, N.S., Leys, D. & Munro, A.W.

Biochemical Society Transactions., 34, 1173-1177, DOI: 10.1042/BST0341173

[180] α-secondary isotope effects as probes of ‘tunneling-ready’ configurations in enzymatic H-tunneling: insight from environmentally coupled tunneling models (2006)

Pudney, C. R., Hay, S., Sutcliffe, M. J., & Scrutton, N. S.

Journal of the American Chemical Society 128, 14053-14058,DOI: 10.1021/ja0614619

[179] Hydrogen tunneling in enzyme-catalyzed hydrogen transfer: aspects from flavoprotein catalysed reactions (2006)

Basran, J., Hothi, P., Masgrau, L., Sutcliffe, M. J. & Scrutton, N. S.

Handbook of Hydrogen Transfer Vol 2, Biological aspects of H-transfer (Eds, Klinman, J.P. & Schowen, R. L.). Wiley. pp. 1341-1359. DOI: 10.1002/9783527611546.ch42

[178] Mechanism of FAD reduction and the role of the active site residues His-225 and Tyr-259 in Arthrobacter globiformis dimethylamine dehydrogenase: analysis of mutant structure and catalytic function (2006)

Basran, J., Fullerton, S., Leys, D. & Scrutton, N. S.

Biochemistry, 45, 11151-11161 , DOI: 10.1021/bi061094d

[177] Hydrogen tunnelling in enzyme-catalyzed H transfer reactions: flavoprotein and quinoprotein systems (2006)

Sutcliffe, M. J., Masgrau, L., Roujeinikova, A., Johannissen, L. O., Hothi, P., Basran, J., Ranaghan, K. E., Mulholland, A. J., Leys, D. & Scrutton, N. S.

Philosophical Transactions of the Royal Society B., 361, 1375-1386.

[176] Introduction: Quantum catalysis in enzymes – beyond the transition state theory paradigm (2006)

Dutton, P. L., Munro, A. W., Scrutton, N. S. & Sutcliffe, M.,

Philosophical Transactions of the Royal Society B., 361, 1293-1294, DOI: 10.1098/rstb.2006.1879

[175] Magnetic field effects and radical pair mechanisms in enzymes: reappraisal of the horseradish peroxidase system (2006)

Jones, A. R., Scrutton, N. S. & Woodward, J.

Journal of the American Chemical Society, 128, 8408-8409, DOI: 10.1021/ja060463q

[174] Lys-D48 is required for charge stabilization, rapid flavin reduction and internal electron transfer in the catalytic cycle of dihydroorotate dehydrogenase B of Lactococcus lactis (2006)

Combe, J. P., Basran, J., Hothi, P., Leys, D., Rigby, S. E. J., Munro, A. W. & Scrutton, N. S.

Journal of Biological Chemistry, 281, 17977-17988, DOI: 10.1074/jbc.M601417200 Free Access

[173] Quantum catalysis in enzymes – beyond the transition state theory paradigm (2006)

Scrutton, N. S., Sutcliffe, M. J. & Dutton, P. L.

Journal of the Royal Society. Interface, 3, 465-469.

[172] Atomic description of an enzyme reaction dominated by proton tunnelling (2006)

Masgrau, L., Roujeinikova, A., Johannissen, L. O., Basran, J., Ranaghan, K., Hothi, P., Mulholland, A., Sutcliffe, M. J., Scrutton, N. S. & Leys, D.

Science 312, 237-241, DOI: 10.1126/science.1126002

[171] Computational studies of enzyme mechanism: linking theory with experiment in the analysis of enzymic H-tunnelling (2006)

Sutcliffe, M. J. & Scrutton, N. S.

Phys. Chem. Chem. Phys., 8, 4510-4516, DOI: 10.1039/B609622K

[170] Analysis of flavin dynamics and thermodynamics using EPR and potentiometric methods (2005)

Dunford, A.J., Rigby, S.E.J., Munro, A.W. & Scrutton, N.S.

Flavins and Flavoproteins; Proceedings of the Fifteenthh International Symposium, Shonan Village, Japan, (Ed.s T. Nishino, R. Miura, M. Tanokura, K. Fukui), ARchiTect Inc., Tokyo, pp. 473–478

[169] Lys-300 plays a major role in the catalytic mechanism of maize polyamine oxidase (2005)

Polticelli, F., Basran, J., Faso, C., Cona, A., Minervini, G., Angelini, R. Federico, R., Scrutton, N. S. & Tavladoraki, P.

Biochemistry, 44, 16108-16120, DOI: 10.1021/bi050983i

[168] TTQ cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis: cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans (2005)

Hothi, P., Abu Khadra, K., Combe, J. P., Leys, D. & Scrutton, N. S.

FEBS Journal, 272, 5894-5909, DOI: 10.1111/j.1742-4658.2005.04990.x Free Access

[167] The dimeric form of flavocytochrome P450 BM3 is catalytically functional as a fatty acid hydroxylase (2005)

Neeli, R., Girvan, H. M., Lawrence, A., Warren, M. J., Leys, D., Scrutton, N. S. & Munro, A. W.

FEBS Letters., 579, 5582-5588, DOI: 10.1016/j.febslet.2005.09.023 Free Access

[166] The human apoptosis-inducing protein AMID is an oxidoreductase with a modified flavin cofactor and DNA binding activity (2005)

Marshall, K.R., Gong, M., Wodke, L., Lamb, J. H., Jones, D. J. L., Farmer, P. B., Scrutton, N. S. and Munro, A. W.

Journal of Biological Chemistry., 280, 30735-30740, DOI: 10.1074/jbc.M414018200 Free Access

[165] Proton transfer in pentaerythritol tetranitrate reductase: structure of the reduced enzyme-progesterone complex and roles of Tyr-186, His-181 and His-184 (2005)

Khan, H., Barna, T., Bruce, N. C., Munro, A. W., Leys, D. & Scrutton, N. S.

FEBS Journal, 272, 4660-4671, DOI: 10.1111/j.1742-4658.2005.04875.x Free Access

[164] Stabilisation of non-productive conformations underpins rapid electron transfer to ETF (2005)

Toogood, H. S., van Thiel, A., Scrutton, N. S. & Leys, D.

Journal of Biological Chemistry., 280, 30361-30366, DOI: 10.1074/jbc.M505562200 Free Access

[163] Biodiversity of cytochrome P450 redox systems (2005)

McLean, K.J., Sabri, M., Marshall, K.R., Lawson, R.J., Lewis, D.G., Clift, D., Balding, P.R., Dunford, A.J.,Warman, A.J., McVey, J.P., Quinn, A.M., Scrutton, N.S. & Munro, A.W.

Biochemical Society Transactions., 33, 796-801, DOI: 10.1042/BST0330796

[162] Crystal structure of DMGO provides a prototype for a new tetrahydrofolate binding fold (2005)

Scrutton, N. S. & Leys, D.

Biochemical Society Transactions., 33, 776-779, DOI: 10.1042/BST0330776

[161] Flavoenzyme catalysed oxidation of amines: roles for flavin and protein-based radicals (2005)

Rigby, S. E., Basran, J., Combe, J. P., Mohsen, A. A., Toogood, H. S., van Thiel, A., Sutcliffe, M. J., Leys, D., Munro, A. W. & Scrutton, N. S.

Biochemical Society Transactions. 33, 754-757, DOI: 10.1042/BST0330754

[160] Flavocytochrome P450 BM3: an update on structure and mechanism of a biotechnologically important enzyme (2005)

Warman, A.J., Roitel, O., Neeli, R., Girvan, H.M., Seward, H.E., Murray, S.A., McLean, K.J., Joyce, M.G., Toogood, H., Holt, R.A., Leys, D., Scrutton, N.S. & Munro, A.W.

Biochemical Society Transactions., 33, 747-753, DOI: 10.1042/BST0330747

[159] Crystallisation and preliminary diffraction analysis of a flavoenzyme amine dehydrogenase/oxidase from Pyrococcus furiosus DSM 3638 (2005)

Monaghan, P. J., Leys, D. & Scrutton, N. S.

Acta Cryst, F61, 756-758, DOI: 10.1107/S1744309105020737 Open Access

[158] Role of active site residues and solvent in proton transfer and the modulation of flavin reduction potential in bacterial morphinone reductase (2005)

Messiha, H. L., Bruce, N. C., Sattelle, B. M., Sutcliffe, M. J., Munro, A. W. & Scrutton, N. S.

Journal of Biological Chemistry., 280, 27103-27110, DOI: 10.1074/jbc.M502293200 Free Access

[157] Kinetic isotope effects and ligand binding in PQQ-dependent methanol dehydrogenase (2005)

Hothi, P., Sutcliffe, M. J. & Scrutton, N. S.

Biochem. J., 388, 123-133, DOI: 10.1042/BJ20041731

[156] Switching pyridine nucleotide specificity in flavocytochrome P450 BM3 (2005)

Neeli, R., Roitel, O., Scrutton, N. S. & Munro, A. W.

Journal of Biological Chemistry., 280, 17634-17644, DOI: 10.1074/jbc.M413826200 Free Access

[155] Reaction of morphinone reductase with 2-cyclohexen-1-one and 1-nitrocyclohexene: proton donation, ligand binding and the role of residues His-186 and Asn-189 (2005). Messiha, L. F., Munro, A. W., Bruce, N. C., Barsukov, I & Scrutton, N. S.,Journal of Biological Chemistry, 280, 10695-10709, DOI: 10.1074/jbc.M410595200 Free Access

[154] A stable tyrosyl radical in monoamine oxidase A (2005)

Rigby, S. E. J., Hynson, R. M. G., Ramsay, R. R., Munro, A. W. & Scrutton, N. S.

Journal of Biological Chemistry., 280, 4627-4631, DOI: 10.1074/jbc.M410596200 Free Access

[153] Solution and computational studies of kinetic isotope effects in flavoprotein and quinoprotein catalyzed substrate oxidations as probes of enzymic hydrogen tunneling and mechanism (2005)

Basran, J., Masgrau, L., Sutcliffe, M. J. & Scrutton, N. S.

Isotope Effects in Chemistry and Biology (Eds. Kohen, A. & Limbach, H.). pp. 671-689

[152] Electron transfer partners of cytochrome P450. (2005)

Paine, M., Scrutton, N. S., Munro, A. W., Gutierrez, A., Roberts, G. C. K. & Wolf, C. R.

Cytochromes P450: Structure, Mechanism, and Biochemistry (3rd Edition) (Ed. Ortiz de Montellano) Kluwer Academic/Plenum Publishers. New York. pp. 115-148, DOI: 10.1007/0-387-27447-2_4

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