2010 - 2014 Publications

[332] Magnetic field effects as a result of the radical pair mechanism are unlikely in redox enzymes (2014)

Messiha, H. L., Wongnate, T., Chaiyen, P., Jones, A. R. & Scrutton N. S.,

Journal of the Royal Society. Interface, 12, 20141155 DOI: 10.1098/rsif.2014.1155 Open Access

[331] A conformational sampling model for radical catalysis in PLP- and cobalamin-dependent enzymes (2014)

Menon, B., Fisher, K., Rigby, S. E. J., Scrutton, N. S. & Leys, D.

Journal of Biological Chemistry, 289, 34161-34174, DOI: 10.1074/jbc.M114.590471 Open Access

[330] Comprehensive analysis of the green to blue photoconversion of full-length cyanobacteriochrome Tlr0924 (2014)

Hardman, S. J.O., Hauck, A. F. E. Clark, I. P., Heyes, D. J. & Scrutton, N. S.

Biophysical. Journal, 107, 2195–2203, DOI: 10.1016/j.bpj.2014.09.020 Open Access

[329] Quantum mechanics/molecular mechanics studies of the mechanism of action of cofactor pyridoxal 5’-phosphate in ornithine 4,5-aminomutase (2014)

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

Chemistry, A European Journal, 20, 11390-11401, DOI: 10.1002/chem.201402759

[328] Cryptochrome-dependent magnetic field effect on seizure response in Drosophila larvae (2014)

Marley, R., Giachello, C. N. G., Scrutton, N. S., Baines, R. A. & Jones, A. R.

Scientific Reports., 4, 5799, DOI: 10.1038/srep05799 Open Access

[327] Conformational change in cytochrome P450 reductase adsorbed at a Au(110)/phosphate buffer interface induced by interaction with nicotinamide adenine dinucleotide phosphate (2014)

Smith, C. I., Convery, J. H., Khara, B., Scrutton, N. S. & Weightman, P.

Physical Review E., 90, 022708, DOI: 10.1103/PhysRevE.90.022708

[326] Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase (2014)

Leferink, N., Antonyuk, S. V., Houwman, J. A., Scrutton, N. S., Eady, R. R. & Hasnain, S. S.

Nature Communications, 5, 4395, DOI: 10.1038/ncomms5395 Open Access

[325] The photoinitiated reaction pathway of full-length cyanobacteriochrome Tlr0924 monitored over 12 orders of magnitude (2014)

Hauck, A. F. E., Hardman, S. J. O., Kutta, R. J., Greetam, G. M., Towrie, M., Heyes, D. J. & Scrutton, N. S.

Journal of Biological Chemistry, 289, 17747-17757, DOI: 10.1074/jbc.M114.566133 Open Access

[324] Nanofibrillar peptide hydrogels for the immobilization of biocatalysts for chemical transformations (2014)

Hickling, C., Toogood, H. S., Saiani, A., Scrutton, N. S. & Miller, A. F.

Macromolecular Rapid Communications 35, 868-874, DOI: 10.1002/marc.201400027 Open Access

[323] Energy landscapes and catalysis in nitric oxide synthase (2014)

Sobolewska-Stawiarz, A., Leferink, N. G. H., Fisher, K., Heyes, D.J., Hay, S., Rigby, S. E. J. & Scrutton, N. S.,

Journal of Biological Chemistry, 289, 11725-11738, DOI: 10.1074/jbc.M114.548834 Open Access

[322] New developments in ‘ene’ reductase catalysed biological hydrogenations (2014)

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

Current Opinion in Chemical Biology, 19, 107-115, DOI: 10.1016/j.cbpa.2014.01.019

[321] Alternative hydride sources for ‘ene’ reductases: current trends (2014)

Toogood, H. S., Knaus, T. & Scrutton, N. S.

ChemCatChem., 6, 951-954, DOI: 10.1002/cctc.201300911 Open Access

[320] Origin of the proton-transfer step in the cofactor-free 1-H-3-hydroxy-4-oxoquinaldine 2,4- dioxygenase: Effect of the basicity of an active site His residue (2014)

Hernandez-Ortega, A., Quesne, M. H., Bui, S., Heuts, N., Steiner, R., Heyes, D. J., de Visser, S. P. & Scrutton, N. S.

Journal of Biological Chemistry. 289, 8620-8632, DOI: 10.1074/jbc.M113.543033 Open Access

[319] Practical aspects on the use of kinetic isotope effects as probes of flavoprotein enzyme mechanisms (2014) Pudney, C. R., Hay, S. & Scrutton, N. S., Methods Mol. Biol., 1146, 161-175, DOI: 10.1007/978-1-4939-0452-5_8

[318] The influence of the structure of the Au(110) surface on the ordering of monolayers and bilayers of cytochrome P450 reductase at the Au(110)/phosphate buffer interface (2014)

Smith, C., Convery, J.H., Khara, B., Scrutton, N. S. & Weightman, P.

Phys. Stat. Sol. B. Basic Solid State Physics, 251, 549-554, DOI: 10.1002/pssb.201350063 Open Access

[317] Proton tunnelling and promoting vibrations during the oxidation of ascorbate by ferricyanide? (2014)

Kandathil, S. M., Driscoll, M., Dunn, R. M., Scrutton, N. S. & Hay, S.

Phys Chem Chem Phys., 16, 2256-2259, DOI: 10.1039/C3CP55131H Open Access

[316] Proton-Coupled Electron Transfer and Adduct Configuration Are Important for C4a-Hydroperoxyflavin Formation and Stabilization in a Flavoenzyme (2014)

Wongnate, T., Surawatanawong, P., Visitsatthawong, S., Sucharitakul, J., Scrutton, N. S. & Chaiyen, P.

Journal of the American Chemical Society, 136, 241-253, DOI: 10.1021/ja4088055 Open Access

[315] Excited state dynamics can be used to probe donor-acceptor distances for H-tunneling reactions catalysed by flavoproteins (2013)

Hardman, S. J. O., Pudney, C. R., Hay, S. & Scrutton, N. S.,

Biophysical Journal, 105, 2549-2558, DOI: 10.1016/j.bpj.2013.10.015 Free Access

[314] Modulation of ligand-heme reactivity by binding pocket residues demonstated in cytochrome c’ over the femtosecond to second temporal range (2013)

Russell, H. J., Hardman, S. J. O., Heyes, D. J., Hough, M. A., Greetham, G. M., Towrie, M., Hay, S. & Scrutton, N. S.

FEBS Journal, 280, 6070-6082, 10.1111/febs.12526 Open Access

[313] Conformational change induced by electron transfer in a monolayer of cytochrome P450 reductase adsorbed at the Au(110)/phosphate buffer interface (2013)

Weightman, P., Smith, C. I., Convery, J. H., Harrison, P., Khara, B. & Scrutton, N. S.,

Physical Review E. 88, 032715, DOI: 10.1103/PhysRevE.88.032715 Open Access

[312] Dynamic-electrostatic model for the generation and control of high energy, radical intermediates by a coenzyme B12-dependent enzyme (2013)

Chen, Z-G., Ziętek, M. A., Russell, H. J. Tait, S., Hay, S., Jones, A. J. & Scrutton, N. S.

ChemBioChem, 14, 1529-1533,DOI: 10.1002/cbic.201300420 Open Access

[311] Production of propane and other short chain alkanes by structure-based engineering of ligand specificity in aldehyde-deformylating oxygenase (2013)

Khara, B., Menon, N., Levy C., Mansell, D., Das, D., Marsh, E. N. G., Leys, D. & Scrutton, N. S.,

ChemBioChem, 14, 1204-1209, DOI: 10.1002/cbic.201300307 Open Access

[310] Relating localised protein motions to the reaction coordinate in coenzyme B12-dependent enzymes (2013)

Jones, A.R., Levy, C., Hay, S. & Scrutton, N. S.,

FEBS Journal 280, 2997-3008, DOI: 10.1111/febs.12223 Free Access

[309] Special issue: catalytic mechanisms by biological systems (2013)

Fraaije, M. W. & Scrutton, N. S.

FEBS Journal 280, 2947, DOI: 10.1111/febs.12317 Free Access

[308] Enzyme engineering toolbox – a ‘catalyst’ for change (2013)

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

Catalysis Science & Technology, 3, 2182-2194, DOI: 10.1039/C3CY00202K

[307] The causative role and therapeutic potential of the kynurenine pathway in neurodegenerative disease (2013)

Amaral, M., Outiero, T. F., Scrutton, N. S. & Giorgini, F.

Journal of Molecular Medicine 91, 705-713, DOI: 10.1007/s00109-013-1046-9

[306] Structural basis of kynurenine 3-monooxygenase inhibition (2013)

Amaral, M., Levy, C., Heyes, D. J., Lafite, P., Outeiro, T., Giorgini, F., Leys, D. & Scrutton, N. S.,

Nature, 496, 382-385, DOI: 10.1038/nature12039

[305] Updated structure of Drosophila cryptochrome (2013)

Levy, C., Zoltowski, B. D., Jones, A. J., Vaidya, A. T., Top D., Widom, J., Young, M. W, Scrutton, N. S., Crane, B. R. & Leys, D.

Nature, 495, E3-4, DOI: 10.1038/nature11995

[304] Enzyme single molecule kinetic isotope effects (2013)

Pudney, C. R., Lane, R., Fielding, A. J., Magennis, S. W., Hay, S. & Scrutton, N. S.,

Journal of the American Chemical Society, 135, 3855-3864, DOI:10.1021/ja309286r

[303] Biocatalytic asymmetric alkene reduction: crystal structure and characterization of a double bond reductase from Nicotiana tabacum (2013)

Mansell, D.J, Toogood, H.S, Waller, J., Hughes M.X., Levy, C.W., Gardiner, J.M. & Scrutton, N.S.

ACS Catalysis, 3, 370-379, DOI: 10.1021/cs300709m Open Access

[302] Fast protein motions are coupled to enzyme H-transfer reactions (2013)

Pudney, C.R., Guerriero, A., Baxter, N., Johannissen, L. O., Waltho, J. P., Hay, S. & Scrutton, N. S.

Journal of the American Chemical Society, 135, 2512-2517, DOI: 10.1021/ja311277k

[301] Electro-enzymatic viologen-mediated substrate reduction using pentaerythritol tetranitrate reductase and a parallel, segmented fluid flow system (2013)

Fisher, K., Mohr, S., Mansell, D., Goddard, N. J., Fielden, P. R. & Scrutton, N. S.

Catalysis Science & Technology, 3, 1505-1511, DOI: 10.1039/C3CY20720J

[300] Ultrafast red light activation and slow conformational changes trigger the signaling cascade in Synechocystis phytochrome Cph1 (2012)

Heyes, D. J., Khara, B., Sakuma, M., Hardman, S. J. O., O'Cualain, R., Rigby, S. E. J. & Scrutton, N. S.

PloS One., 7, e52418, DOI: 10.1371/journal.pone.0052418 Open Access

[299] Crystal structure of a soluble form of human CD73 with ecto-5’-nucleotidase activity (2012)

Heuts, D.P.H.M., Weissenborn, M.J., Olkhov, R.V., Shaw, A.M., Gummadova, J., Levy, C. & Scrutton, N. S.

ChemBioChem., 13, 2384-2391, DOI: 10.1002/cbic.201200426

[298] A surprising observation that oxygen can affect the product enantiopurity of an enzyme catalysed reaction (2012)

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

FEBS Journal 279, 4160-71, DOI: 10.1111/febs.12008, Free Access Faculty 1000 recommended

[297] Biocatalyst identification by anaerobic high throughput screening of enzyme libraries and anaerobic microorganisms (2012)

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

Protein Engineering Handbook Vol.3 (Eds. Lutz, S & Bornscheuer), Wiley. pp. 193-214

[296] Mechanistic reappraisal of early stage photochemistry in the light-driven enzyme protochlorophyllide oxidoreductase (2012)

Heyes, D. J., Hardman, S. J. O., Mansell, D., Gardiner, J.M. & Scrutton, N. S.

PLoS One. 7:e45642., DOI: 10.1371/journal.pone.0045642.g010 Open Access

[295] Protein motions are coupled to the reaction chemistry in coenzyme B12-dependent ethanolamine ammonia lyase (2012)

Russell, H. J., Jones, A. R., Hay, S., Greetham, G. M., Towrie, M. & Scrutton, N. S.,

Angewandte Chemie International Ed., 51, 9306-9310, DOI: 10.1002/anie.201202502

[294] Controlling the formation of a monolayer of cytochrome P450 reductase onto Au surfaces (2012)

Convery, J. H., Smith, C. I., Khara, B., Scrutton, N. S., Harrison, P., Farrell, T., Martin, T. S. & Weightman, P.

Physical Review E., 86, 011903, DOI: 10.1103/PhysRevE.86.011903

[293] Ultrafast infrared spectral fingerprints of vitamin B12 and related cobalamins (2012)

Jones, A. R., Russell, H. J., Greetham, G. M., Towrie, M. & Scrutton, N. S.

Journal of Physical Chemistry B. 116, 5586-5594, DOI: 10.1021/jp304594d

[292] Pressure effects on enzyme-catalyzed quantum tunneling events arise from protein-specific structural and dynamic changes. (2012)

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

Journal of the American Chemical Society, 134, 9749-9754, DOI: 10.1021/ja3024115

[291] Laser-flash photolysis indicates that internal electron transfer is triggered by proton uptake by Alcaligenes xylosoxidans copper-dependent nitrite reductase (2012)

Leferink, N.G.H., Eady, R.R., Hasnain, S. S. & Scrutton N. S.

FEBS Journal 279, 2174-2181, DOI: 10.1111/j.1742-4658.2012.08601.x Free Access

[290] Kinetic and spectroscopic probes of motions and catalysis in the cytochrome P450 reductase family of enzymes (2012)

Pudney, C. R., Heyes, D. J., Khara, B., Hay, S., Rigby, S. E. J. and Scrutton, N. S.

FEBS Journal, 279, 1534–1544, DOI: 10.1111/j.1742-4658.2011.08442.x Free Access

[289] Human cryptochrome-1 confers light-independent activity in transgenic Drosophila correlated with flavin radical stability (2012)

Vieira, J., Jones, A. R., Danon, A., Sakuma, M., Hoang, N., Robles, D., Tait , S., Heyes, D. J., Picot, M., Yoshii, T., Helfrich-Foerster, C., Soubigou, G., Coppee, J-Y., Klarsfeld, A., Rouyer, F., Scrutton, N. S. & Ahmad, M.

PloS One., e31867, DOI: 10.1371/journal.pone.0031867 Open Access

[288] Enantioselective bioreduction of carbon-carbon double bonds (2012)

Toogood, H. S., Mansell, D., Gardiner, J. M. & Scrutton, N. S.

Comprehensive Chirality Vol 7 (Ed. Turner N. J.) Elsevier, pp. 216-255, DOI: 10.1016/B978-0-08-095167-6.00713-8

[287] 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(2012)

Leferink, N. G. H., Pudney, C. R., Brenner, S., Heyes, D. J., Eady, R. R., Hasnain, S. S., Hay, S., Rigby, S. E. J. & Scrutton, N. S.

FEBS Letts., 586, 578-584, DOI: 10.1016/j.febslet.2011.07.003 Free Access

[286] Good vibrations in enzyme catalysed reactions (2012)

Hay, S & Scrutton N. S.

Nature Chemistry 4, 161-168, DOI: 10.1038/nchem.1223

[285] Large-scale domain conformational change is coupled to the activation of the Co-C bond in the B12-dependent enzyme ornithine 4,5-aminomutase: a computational study (2012)

Pang, J., Li, X., Morokuma, K., Scrutton, N. S. & Sutcliffe, M. J.

Journal of the American Chemical Society, 134, 2367-77, DOI: 10.1021/ja210417k

[284] Role of His 225 in radical stabilization and catalysis in ornithine 4,5 aminomutase (2012)

Makins, C., Miros, F., Scrutton, N. S. & Wolthers, K. R.,

Bioorganic Chemistry, 40, 39-47, DOI: 10.1016/j.bioorg.2011.08.003

[283] Excited state dynamics and catalytic mechanism of the light-driven enzyme protochlorophyllide oxidoreductase (2012)

Scrutton, N. S., Groot, M. L. & Heyes, D. J.

Phys. Chem. Chem. Phys., 14, 8818-8824, DOI: 10.1039/C2CP23789J

[282] Experimental approaches towards proton-coupled electron transfer reactions in biological redox systems (2011)

Brenner, S., Hay, S. Derren J. Heyes & Scrutton, N. S.

‘Proton coupled electron transfer’ (Eds. Formosinho, F., Barroso, M.) RSC publishing, pp. 57 -88

[281] Tryptophan 697 controls hydride and interflavin electron transfer in human methionine synthase reductase (2011)

Meints, C., Gustaffson, F. S., Scrutton, N. S. & Wolthers, K. R.

Biochemistry, 50, 11131-11142, DOI: 10.1021/bi2012228

[280] Coupled motions direct electrons along human microsomal P450 chains (2011)

Pudney, C. R., Khara, B., Johannissen, L. O. & Scrutton, N. S.

PloS Biol. e1001222, DOI: 10.1371/journal.pbio.1001222 Open Access

[279] Examining the importance of dynamics, barrier compression and hydrogen tunneling in enzyme catalysed reactions (2011)

Hay, S & Scrutton, N. S.,

Procedia Chemistry, 22nd Solvay Conference on Chemistry, 3, 306-315, DOI: 10.1016/j.proche.2011.08.038

[278] CO poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins (2011)

Antonyuk, S., Rustage, N., Peterson, C. A., Arnst, J. L., Heyes, D. J., Sharma, R., Berry, N., Scrutton, N. S., Eady, R. R., Andrew, C. R & Hasnain, S. S.

Proc. Natl. Acad. Sci. USA, 108, 15780-15785, DOI: 10.1073/pnas.1109051108

[277] Reaction of vascular adhesion protein-1 with primary amines: mechanistic insights from isotope effects and quantitative structure-activity relationships (2011)

Heuts, D. P. H. M., Gummadova, J. O., Pang, J., Rigby, S. E. J. & Scrutton, N. S.

Journal of Biological Chemistry, 286, 29584-29593, DOI: 10.1074/jbc.M111.232850 Free Access

[276] Proton coupled electron transfer in the catalytic cycle of Alcaligenes xylosoxidans copper-dependent nitrite reductase (2011)

Leferink, N. G. H., Han, C., Antonyuk, S. V. Heyes, D. J., Rigby, S. E. J., Hough, M. A., Eady, R. R., Scrutton, N. S. & Hasnain, S. S.

Biochemistry, 50, 4121-4131, DOI: 10.1021/bi200246f

[275] ELDOR spectroscopy reveals that energy landscapes in human methionine synthase reductase are extensively remodeled following ligand and partner protein binding (2011)

Rigby, S. E. J., Lou, X., Toogood, H. S., Wolthers, K. R. & Scrutton, N. S.

ChemBioChem., 12, 863-867, DOI: 10.1002/cbic.201000630

[274] A twin-track approach has optimised proton and hydride transfer by dynamically-coupled tunnelling during the evolution of protochlorophyllide oxidoreductase (2011)

Heyes, D.J., Levy, C., Sakuma, M., Robertson, D. L. & Scrutton N. S.

Journal of Biological Chemistry, 286, 11849-11854, DOI: 10.1074/jbc.M111.219626 Free Access

[273] Identification of N-terminal regions of wheat leaf ferredoxin NADP+ oxidoreductase for interactions with ferredoxin (2011)

Bowsher, C., Eyres, L., Gummadova, J., Hothi, P., McLean, K., Munro, A. W., Scrutton, N. S. Hanke, G., Sakakibara, Y. & Hase, T.

Biochemistry, 50, 1778-1787, DOI: 10.1021/bi1014562

[272] A site-saturated mutagenesis study reveals that residues 181 and 184 influence ligand binding, stereochemistry and oxime formation in pentaerythritol tetranitrate reductase (2011)

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

ChemBioChem., 12, 738-749, DOI: 10.1002/cbic.201000662

[271] Active site modifications in pentaerythritol tetranitrate reductase can lead to improved product enantiopurity, decreased by-product formation and altered stereochemical outcome in reactions with a,b-unsaturated nitroolefins (2011)

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

Catalysis Science & Technology, 1, 948-957, DOI: 10.1039/C0CY00092B

[270] Is there a dynamic protein contribution to the substrate trigger in coenzyme B12-dependent ethanolamine ammonia lyase? (2011)

Jones, A. R., Hardman, S. J. O. Hay, S., & Scrutton, N. S.

Angewandte Chemie, 50, 10843-10846, DOI: 10.1002/ange.201105132

[269] How does pressure affect barrier compression and isotope effects in an enzymatic H-tunnelling reaction? (2011)

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

Angewandte Chemie, 50, 2129-2132, DOI: 10.1002/anie.201006668

[268] Focused directed evolution of pentaerythritol tetranitrate reductase using automated anaerobic kinetic screening of site-saturated libraries (2010)

Hulley, M. E., Toogood, H. S., Fryszkowska, A., Mansell, D., Stephens, G. M., Gardiner, J. M. & Scrutton, N. S.

ChemBioChem., 11, 2433-2447, DOI: 10.1002/cbic.201000527

[267] Direct analysis of donor-acceptor distance and relationship to isotope effects and the force constant for barrier compression in enzymatic H-tunneling reactions (2010)

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

Journal of the American Chemical Society, 132, 11329-11335, DOI: 10.1021/ja1048048, Also, see accompanying News and Views Nature Chemistry 2, 907-909 (2010)

[266] Biocatalytic reductions and chemical versatility of the Old Yellow Enzyme family of flavoprotein oxidoreductases (2010)

Toogood, H. S., Gardiner, J. M. & Scrutton, N. S.

ChemCatChem, 2, 892-914, DOI: 10.1002/cctc.201000094

[265] Nature of the energy landscape for gated electron transfer in a dynamic redox protein (2010)

Hay, S., Brenner, S., Khara, B., Quinn, A. M., Rigby, S. E. J & Scrutton, N. S.

Journal of the American Chemical Society, 132, 9738-9745, DOI: 10.1021/ja1016206

[264] Integrating computational methods with experiment uncovers the role of dynamics in enzyme-catalysed H-tunnelling reactions (2010)

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

Kinetics and Dynamics: from Nano- to Bio-scale Challenges and Advances in Computational Chemistry and Physics (Eds. Paneth, P & Dybala-Defratyka, A.) Springer, pp. 501-520, DOI: 10.1007/978-90-481-3034-4_19

[263] Probing enzyme active site geometry using high pressure and secondary isotope effects in an enzyme-catalysed ‘deep’ H-tunneling reaction (2010)

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

Journal of Physical Organic Chemistry, 23, 696-701, DOI: 10.1002/poc.1653

[262] Tyrosyl radical formation and propagation in flavin dependent monoamine oxidases (2010)

Dunn, R. V., Munro, A. W., Turner, N. J., Rigby, S. E. J. & Scrutton, N. S.

ChemBioChem, 11, 1228-1231, DOI: 10.1002/cbic.201000184

[261] Continuous two-phase flow miniaturised bioreactor for monitoring anaerobic biocatalysis by pentaerythritol tetranitrate reductase (2010)

Mohr, S., Fisher, K., Scrutton, N. S., Goddard, N. J. & Fielden, P. R.

Lab Chip,10, 1929-1936, DOI: 10.1039/C003561K

[260] Large-scale domain dynamics and adenosylcobalamin reorientation orchestrate radical catalysis in ornithine 4,5 aminomutase (2010)

Wolthers, K. R., Levy, C., Scrutton, N. S. & Leys, D.

Journal of Biological Chemistry., 285,13942-13950, DOI: 10.1074/jbc.M109.068908 Free Access

[259] New insights into the multi-step reaction pathway of the reductive half-reaction catalysed by aromatic amine dehydrogenase: A QM/MM study (2010)

Pang, J., Scrutton, N. S. de Visser, S. P. & Sutcliffe, M. J.

Chem. Comm., 46, 3104-3106, DOI: 10.1039/C003107K

[258] Biocatalysis with thermostable enzymes: structure and properties of a thermophilic ‘ene’-reductase related to Old Yellow Enzyme (2010)

Adalbjörnsson, B. V., Toogood, H.S., Fryszkowska, A., Pudney, C. R., Jowitt, T. A., Leys, D. & Scrutton, N. S.

ChemBioChem., 11, 197-207, DOI: 10.1002/cbic.200900570

[257] Assignment of the vibrational spectrum of enzyme-bound tryptophan tryptophylquinone using a combined QM/MM approach (2010)

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

Jounral of Physical Chemistry A., 114, 1212-1217, DOI: 10.1021/jp910161k

[256] Mutagenesis alters the catalytic mechanism of the light-driven enzyme protochlorophyllide oxidoreductase (2010)

Menon, B. R. K., Davison, P. A., Hunter, C. N., Scrutton, N. S. & Heyes, D.

Journal of Biological Chemistry, 285, 2113-2119, DOI: 10.1074/jbc.M109.071522 Free Access

[255] Barrier compression and its contribution to both classical and quantum mechanical aspects of enzyme catalysis (2010)

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

Biophysical Journal, 98, 121-128, DOI: 10.1016/j.bpj.2009.09.045 Free Access