Pre-2000 Publications

[80] Colworth Medal lecture 'Enzymes in the quantum world' (1999)

Scrutton, N. S.

Biochem. Soc. Trans., 27, 767-779, DOI: 10.1042/bst0270767

[79] Redox cycles in trimethylamine dehydrogenase and the mechanism of substrate inhibition(1999)

Roberts, P., Basran, J., Wilson, E. K., Hille, R. & Scrutton, N. S.

Biochemistry, 38, 14927-14940, DOI: 10.1021/bi9914098

[78] New insights into enzyme catalysis: ground state tunnelling driven by protein dynamics (1999)

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

Eur. J. Biochem., 264, 666-671, DOI: 10.1046/j.1432-1327.1999.00645.x Free Access

[76] The role of Tyr 169 of trimethylamine dehydrogenase in substrate oxidation and magnetic interaction between FMN cofactor and the 4Fe/4S center (1999)

Basran, J., Jang, M. H., Sutcliffe, M. J., Hille, R. & Scrutton, N. S.

J. Biol. Chem., 274, 13155-13161, DOI: 10.1074/jbc.274.19.13155 Free Access

[75] The reaction of trimethylamine dehydrogenase with trimethylamine (1999)

Jang, M-H., Basran, J. Scrutton, N. S. & Hille, R.

J. Biol. Chem., 274, 13147-13154, DOI: 10.1074/jbc.274.19.13147 Free Access

[74] Enzymatic H-transfer requires vibration-driven extreme tunneling (1999)

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

Biochemistry, 38, 3218-3222, DOI: 10.1021/bi982719d

[73] Electron transfer in trimethylamine dehydrogenase and electron transferring flavoprotein (1999)

Scrutton, N.S., Basran, J., Wilson, E.K., Chohan, K.K., Jang, M-H., Sutcliffe, M.J. & Hille, R.

Biochem. Soc. Trans., 27, 196-200, DOI: 10.1042/bst0270196

[72] Investigating the mechanism of C-H bond breakage in heterotetrameric sarcosine oxidase from Arthrobacter sp 1-IN (1999)

Harris, R. J., Scrutton, N. S., Sutcliffe, M. J. & Meskys, R.

Flavins and Flavoproteins; Proceedings of the Thirteenth International Symposium, Konstanz, Germany (Eds. Ghisla, S, Kroneck, P., Macheroux, P. & Sund, H) pp. 447-450

[71] Structure and mechanism of an explosives-degrading enzyme: PETN reductase(1999)

Barna, T., Moody, P. C. E., Craig, D. H., Bruce, N. C. & Scrutton, N. S.

Flavins and Flavoproteins; Proceedings of the Thirteenth International Symposium, Konstanz, Germany (Eds. Ghisla, S, Kroneck, P., Macheroux, P. & Sund, H) pp. 671-674

[70] The Old Yellow Enzyme family of flavoenzymescomparison of substrate specificity and activity against explosives (1999)

Williams, R. E., Rathbone, D., Scrutton, N. S., Moody, P. C. E., Nicklin, S. & Bruce, N. C.

Flavins and Flavoproteins; Proceedings of the Thirteenth International Symposium, Konstanz, Germany (Eds. Ghisla, S, Kroneck, P., Macheroux, P. & Sund, H) pp. 663-666

[69] Formation of W3A1 ETF hydroquinone in the TMADH/ETF protein complex (1999)

Jang, M.-H., Scrutton, N. S. & Hille, R.

Flavins and Fflavoproteins; Proceedings of the Thirteenth International Symposium, Konstanz, Germany (Eds. Ghisla, S, Kroneck, P., Macheroux, P. & Sund, H) pp. 223-226

[68] The reductive half-reaction of trimethylamine dehydrogenase with trimethylamine (1999)

Jang, M.-H., Basran, J., Hille, R. & Scrutton, N. S.

Flavins and Flavoproteins; Proceedings of the Thirteenth International Symposium, Konstanz, Germany (Eds. Ghisla, S, Kroneck, P., Macheroux, P. & Sund, H) pp. 451-454

[67] Hydrogen tunnelling in amine dehydrogenases from methylotrophic bacteria (1999)

Basran, J., Roberts, P., Scrutton, N. S. & Sutcliffe, M. J.

Flavins and Flavoproteins; Proceedings of the Thirteenth International Symposium, Konstanz, Germany (Eds. Ghisla, S, Kroneck, P., Macheroux, P. & Sund, H) pp. 443-446

[66] Substrate inhibition in trimethylamine dehydrogenase (1999)

Roberts, P., Basran, J., Wilson, E. K., Scrutton, N. S. & Hille, R.

Flavins and Flavoproteins; Proceedings of the Thirteenth International Symposium, Konstanz, Germany (Eds. Ghisla, S, Kroneck, P., Macheroux, P. & Sund, H) pp. 423-426

[65] Structure and mechanism of an opiate-transforming enzyme: morphinone reductase. (1999)

Moody, P. C. E., Craig, D. H., Scrutton, N. S., Munro, A. W., Chapman, S. K. & Bruce, N. C.

Flavins and Flavoproteins; Proceedings of the Thirteenth International Symposium, Konstanz, Germany (Eds. Ghisla, S, Kroneck, P., Macheroux, P. & Sund, H.) pp. 667-670

[64] Identification of covalent flavoproteins and analysis of the covalent link (1999)

Scrutton, N.S.

Flavoprotein Protocols, Methods in Molecular Biology vol 131 (Eds. Chapman, S.K. & Reid, G.A.), Humana press. pp. 181-193, DOI: 10.1385/1-59259-266-X:181

[63] Electron transfer from flavin to iron in the Pseudomonas oleovorans rubredoxin reductase-rubredoxin electron transfer complex (1998)

Lee, H. J., Basran, J. & Scrutton, N. S.

Biochemistry, 37, 15503-15512, DOI: 10.1021/bi981853v

[62] Major structural reorganisation most likely accompanies the transient formation of a physiological electron transfer complex (1998)

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

Protein & Peptide Lett., 5, 231-236

[61] Crystallization and preliminary diffraction studies of pentaerythritol tetranitrate reductase (1998)

Moody, P. C. E., Shikotra, N., French, C. E., Bruce, N. C. & Scrutton, N. S.

Acta Cryst., D54, 675-677, DOI: 10.1107/S0907444997017836

[60] Probing the stabilising role of C-terminal residues in trimethylamine dehydrogenase (1998)

Ertughrul, O. W. D., Errington, N., Raza, S., Sutcliffe, M. J., Rowe, A. J. & Scrutton, N. S.

Protein Eng., 11, 447-455, DOI: 10.1093/protein/11.6.447 Free Access

[59] Reductive and oxidative half-reactions of morphinone reductase from Pseudomonas putida M10: a kinetic and thermodynamic analysis (1998)

Craig, D. H., Moody, P. C. E., Bruce, N. C. & Scrutton, N. S.

Biochemistry, 37, 7598-7607, DOI: 10.1021/bi980345i

[58] Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: the current state of affairs. (1998)

Mewies, M., McIntire, W. S. & Scrutton, N. S.

Protein Science, 7, 1-14, DOI: 10.1002/pro.5560070102 Free Access

[56] Crystallization and preliminary diffraction studies of morphinone reductase, a flavoprotein involved in the degradation of morphine alkaloids (1997)

Moody, P. C. E., Shikotra, N., French, C. E., Bruce, N. C. & Scrutton, N. S.

Acta Cryst., D53, 619-621, DOI: 10.1107/S0907444997004046

[54] Low temperature solution behaviour of Methylophilus methylotrophus electron transferring flavoprotein: a study by analytical ultracentrifugation (1997)

Colfen, H., Harding, S. E., Wilson, E. K., Scrutton, N. S. & Winzor, D.

Eur. Biophys. J., 25, 411-416, DOI: 10.1007/s002490050054

[53] Selective modification of alkyl-ammonium ion specificity in trimethylamine dehydrogenase by the rational engineering of cation-pi bonding (1997)

Basran, J., Mewies, M., Mathews, F. S. & Scrutton, N. S.

Biochemistry, 36, 1989-1998, DOI: 10.1021/bi962623o

[52] An ultracentrifugal approach to quantitative characterisation of the molecular assembly of a physiological electron transfer complex: the interaction of electron transferring flavoprotein with trimethylamine dehydrogenase (1997)

Wilson, E. K, Scrutton, N. S., Colfen, H., Harding, S. E., Jacobsen, M. P. & Winzor, D. J.

Eur. J. Biochem., 243, 393-399, DOI: 10.1111/j.1432-1033.1997.0393a.x Free Access

[51] An exposed tyrosine on the surface of trimethylamine dehydrogenase facilitates electron transfer to electron transferring flavoprotein: kinetics of transfer in wild-type and mutant complexes (1997)

Wilson, E. K., Huang, L., Sutcliffe, M. J. Mathews, F. S., Hille, R. & Scrutton , N. S.

Biochemistry, 36, 41-48, DOI: 10.1021/bi961224q

[50] Trimethylamine dehydrogenase: mechanism and assembly of a complex iron-sulfur flavoprotein (1996)

Scrutton, N. S., Wilson, E. K., Mewies, M., Packman, L. C., Mathews, F. S., Huang, L. & Hille, R.

Flavins and flavoproteins; Proceedings of the Twelfth International Symposium Calgary, Alberta, Canada (Eds. K. Stevenson, V. Massey & C. H. Williams Jr) Walter de Gruyter & Co., Berlin. pp. 857-864

[49] Molecular recognition of organic ammonium cations by di- and trimethylamine dehydrogenases (1996)

Basran, J., Mewies, M., Yang, C-C & Scrutton, N. S.

Flavins and Flavoproteins; Proceedings of the Twelfth International Symposium Calgary, Alberta, Canada (Eds. K. Stevenson, V. Massey & C. H. Williams Jr) University of Calgary Press, pp. 869-872

[48] Rubredoxin/rubredoxin reductase of Pseudomonas oleovorans: a model system for investigating interprotein electron transfer (1996)

Lee, H. J., Lian, L-Y. & Scrutton, N. S.

Flavins and Flavoproteins; Proceedings of the Twelfth International Symposium Calgary, Alberta, Canada (Eds. K. Stevenson, V. Massey & C. H. Williams Jr) University of Calgary Press, pp. 539-544

[47] Electron transfer complex assembly: the association of trimethylamine dehydrogenase with electron transferring flavoprotein (1996)

Wilson, E. K., Scrutton, N. S., Mathews, F. S., Huang, L. & Hille, R.

Flavins and Flavoproteins; Proceedings of the Twelfth International Symposium Calgary, Alberta, Canada (Eds. K. Stevenson, V. Massey & C. H. Williams Jr) University of Calgary Press, pp. 957-960

[46] Crystal structures of recombinant wild-type and a C30A mutant of trimethylamine dehydrogenase from Methylophilus W3A1 (1996)

Mathews, F. S., Trickey, P., Barton, J., Chen, Z-W. & Scrutton, N. S.

Flavins and Flavoproteins; Proceedings of the Twelfth International Symposium Calgary, Alberta, Canada (Eds. K. Stevenson, V. Massey & C. H. Williams Jr) University of Calgary Press, pp. 873-878

[44] Electron transfer in trimethylamine dehydrogenase: directed mutagenesis of a potential tunneling pathway (1996)

Wilson, E. K., Hille, R., Huang, L., Mathews, F. S. & Scrutton, N. S.

Biochem. Soc. Trans., 24, 456S, DOI: 10.1042/bst024456s

[43] Rubredoxin/rubredoxin reductase of Pseudomonas oleovorans: a model system for investigating interprotein electron transfer (1996)

Lee, H. J., Lian, L-Y. & Scrutton, N. S.

Biochem. Soc. Trans., 24, 447S, DOI: 10.1042/bst024447s

[41] Reaction of the C30A mutant of trimethylamine dehydrogenase with diethylmethylamine (1996)

Huang, L., Scrutton, N. S. & Hille, R.

J. Biol. Chem., 271, 13401-13406 Free Access

[40] The reaction of the C30A mutant of trimethylamine dehydrogenase with diethylmethylamine (1996)

Huang, L. X., Scrutton, N. S. & Hille, R.

FASEB J., 10, 6, 2927

[39] Homodimeric and expanded behaviour of trimethylamine dehydrogenase in solution at different temperatures (1996)

Colfen, H., Harding, S. E., Wilson, E. K., Packman, L. C. & Scrutton, N. S.

Eur. Biophys. J., 24, 159-164, DOI: 10.1007/BF00180273

[38] Protein recognition of ammonium cations using side-chain aromatics: a structural variation for secondary ammonium ligands (1995)

Raine, A. R. C., Yang, C-C, Packman, L. C., White, S. A., Mathews, F. S., & Scrutton, N. S.

Protein Science, 4, 2625-2628, DOI: 10.1002/pro.5560041222 Free Access

[37] Altering kinetic mechanism and enzyme stability by mutagenesis of the dimer interface of glutathione reductase (1995)

Bashir, A., Perham, R. N., Scrutton, N. S. & Berry, A.

Biochem. J, 312, 527-533

[36] Dissection of the FMN-binding site in trimethylamine dehydrogenase (1995)

Mewies, M., Packman, L. C. & Scrutton, N. S.

Biochem. Soc. Trans., 23, 509S, DOI: 10.1042/bst023509s

[35] The primary structure of Hyphomicrobium X dimethylamine dehydrogenase: relationship to trimethylamine dehydrogenase and implications for substrate recognition (1995)

Yang, C-C, Packman, L. C. & Scrutton, N. S.

Eur. J. Biochem., 232, 264-271, DOI: 10.1111/j.1432-1033.1995.tb20808.x Free Access

[34] The flavinylation reaction of trimethylamine dehydrogenase: analysis by directed mutagenesis and electrospray mass spectrometry (1995)

Packman, L. C., Mewies, M. & Scrutton, N. S.

J. Biol. Chem., 270, 13186-13191, DOI: 10.1074/jbc.270.22.13186 Free Access

[33] Electron tunneling in substrate-reduced trimethylamine dehydrogenase: kinetics of electron transfer and analysis of the tunneling pathway (1995)

Wilson, E. K., Mathews, F. S., Packman, L. C. & Scrutton, N. S.

Biochemistry, 34, 2584-2591, DOI: 10.1021/bi00008a024

[32] On the evolution of alternate core packing in eight-fold β/α barrels (1994)

Raine, A. R. C., Scrutton, N. S. & Mathews, F. S.

Protein Science, 3, 1889-1892, DOI: 10.1002/pro.5560031028 Free Access

[31] Anatomy of an engineered NAD-binding site (1994)

Mittl, P. R. E., Berry, A., Scrutton, N. S., Perham, R. N. & Schulz, G. E.

Protein Science, 3, 1504-1514, DOI: 10.1002/pro.5560030916 Free Access

[30] Assembly of redox centres in the trimethylamine dehydrogenase of bacterium W3A1: properties of the wild-type enzyme and a C30A mutant expressed from a cloned gene in Escherichia coli (1994)

Scrutton, N. S., Packman, L. C., Mathews, F. S., Rohlfs, R. J. & Hille, R.

J. Biol. Chem., 269, 13942-13950 Free Access

[29] Flavinylation of the trimethylamine dehydrogenase of bacterium W3A1 expressed in Escherichia coli (1994)

Scrutton, N. S., Packman, L. C. & Mathews, F. S.

Flavins and Flavoproteins ; Proceedings of the Eleventh International Symposiym, Nagoya, Japan (Ed. K. Yagi) Walter de Gruyter & Co., Berlin. pp. 803-806

[28] Hybrid molecules of glutathione reductase: tools for investigating protein interactions at the dimer interface (1994)

Scrutton, N. S., Berry, A., Deonarain, M. P. & Perham, R. N.

Flavins and Flavoproteins ; Proceedings of the Eleventh International Symposiym, Nagoya, Japan (Ed. K. Yagi) Walter de Gruyter & Co., Berlin. pp. 485-492

[27] An investigation of engineered cooperativity in mutants of Escherichia coli glutathione reductase (1994)

Bashir, A., Cockerill, M., Berry, A., Scrutton, N. S. & Perham, R. N.

Flavins and Flavoproteins ; Proceedings of the Eleventh International Symposiym, Nagoya, Japan (Ed. K. Yagi) Walter de Gruyter & Co., Berlin. pp.501-504

[26] α/β barrel evolution and the modular assembly of enzymes: emerging trends in the flavin dehydrogenase/oxidase family (1994)

Scrutton, N. S.

BioEssays, 16 115-122, DOI: 10.1002/bies.950160208

[25] Reductive and oxidative half-reactions of glutathione reductase from Escherichia coli (1994)

Rietveld, P., Arscott, L. D., Berry, A., Scrutton, N. S., Deonarain, M. P. Perham, R. N. & Williams, C. H. Jr.

Biochemistry, 33, 13888-13895, DOI: 10.1021/bi00250a043

[24] A designed mutant of the enzyme glutathione reductase shortens the crystallisation time by a factor of forty (1994)

Mittl, P. R. E., Berry, A., Scrutton, N. S., Perham, R. N. & Schulz, G. E.

Acta Cryst., D50, 228-231, DOI:10.1107/S090744499300993X

[23] Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering (1993)

Bocanegra, J. A., Scrutton, N. S. & Perham, R. N.

Biochemistry, 32, 2737-2740, DOI: 10.1021/bi00062a001

[22] Structural differences between wild-type NADP-dependent glutathione reductase from Escherichia coli and a redesigned NAD-dependent mutant (1993)

Mittl, P. R. E., Berry, A., Scrutton, N. S., Perham, R. N. & Schulz, G. E.

J. Mol. Biol., 231, 191-195, DOI: 10.1006/jmbi.1993.1274

[21] Cooperativity induced by a single mutation at the subunit interface of a dimeric enzyme: glutathione reductase (1992)

Scrutton, N. S., Deonarain, M. P., Berry, A. & Perham, R. N.

Science, 258, 1140-1143, DOI: 10.1126/science.1439821

[20] Trimethylamine dehydrogenase of bacterium W3A1. Molecular cloning, sequence determination and over-expression of the gene (1992)

Boyd, G., Mathews, F. S., Packman, L. C. & Scrutton, N. S.

FEBS Lett., 308, 271-276, DOI: 10.1016/0014-5793(92)81291-S Free Access

[19] Engineering surface charge. 2. A method for purifying hetero-dimers of Escherichia coli glutathione reductase (1992)

Deonarain, M. P., Scrutton, N. S. & Perham, R. N.

Biochemistry, 31, 1498-1504, DOI: 10.1021/bi00120a029

[18] Engineering surface charge. 1. A method for detecting subunit exchange in Escherichia coli glutathione reductase (1992)

Deonarain, M. P., Scrutton, N. S. & Perham, R. N.

Biochemistry, 31, 1491-1497, DOI: 10.1021/bi00120a028

[17] New enzymes for old: engineering the substrate and coenzyme specificities of Escherichia coli glutathione reductase (1991)

Perham, R. N., Scrutton, N. S. & Berry, A.

BioEssays, 13, 515-525, DOI: 10.1002/bies.950131005

[16] Engineering the substrate specificity of glutathione reductase toward that of trypanothione reduction (1991)

Henderson, G. B., Murgolo, N. J., Kuriyan, J., Osapay, K., Kominos, D., Berry, A., Scrutton, N. S., Hinchliffe, N. W., Perham, R. N. & Cerami, A.

Proc. Natl. Acad. Sci., USA. 88, 8769-8773

[15] Exploration of the coenzyme and substrate specificity of glutathione reductase and its subunit assembly (1990)

Perham, R. N., Scrutton, N. S., Berry, A. & Deonarain, M. P.

Flavins and Flavoproteins; Proceedings of the Tenth International Symposiym, Como, Italy (Eds. B. Curti, S. Ronchi & G. Zanetti) Walter de Gruyter & Co., Berlin. N.Y. pp. 513-520

[14] Subunit interactions in the glutathione reductase from Escherichia coli (1990)

Berry, A., Deonarain, M. P., Scrutton, N. S. & Perham, R. N.

Flavins and Flavoproteins; Proceedings of the Tenth International Symposiym, Como, Italy (Eds. B. Curti, S. Ronchi & G. Zanetti) Walter de Gruyter & Co., Berlin. N.Y. pp.521-524

[13] Active site mutants of the glutathione reductase from Escherichia coli (1990)

Deonarain, M. P., Scrutton, N. S., Berry, A. & Perham, R. N.

Flavins and Flavoproteins; Proceedings of the Tenth International Symposiym, Como, Italy(Eds. B. Curti, S. Ronchi & G. Zanetti) Walter de Gruyter & Co., Berlin. N.Y. pp.525-528

[12] Active site complementation in engineered hetero-dimers of Escherichia coli glutathione reductase created in vivo (1990)

Scrutton, N. S., Berry, A., Deonarain, M. P. & Perham, R. N.

Proc. Roy. Soc. Lond. B., 242, 217-224, DOI: 10.1098/rspb.1990.0127

[11] Directed mutagenesis of the redox-active disulphide bridge in glutathione reductase of Escherichia coli (1990)

Deonarain, M. P., Scrutton, N. S., Berry, A. & Perham, R. N.

Proc. Roy. Soc. Lond. B., 241, 179-186, DOI: 10.1098/rspb.1990.0083

[10] Redesign of the coenzyme specificity of a dehydrogenase by protein engineering (1990)

Scrutton, N. S., Berry, A. & Perham, R. N.

Nature, 343, 38-43, DOI:10.1038/343038a0

[9] Site-directed mutagenesis and the mechanism of flavoprotein disulphide oxidoreductases. (1989)

Perham, R. N., Berry, A., Scrutton, N. S. & Deonarain, M. P.

Protein structure and engineering, NATO Advanced Science Institutes Series, Series A, Life Science, (Ed. Oleg Jardetzky). Plenum Press, pp. 333-346

[8] Alternative proton donors/acceptors in the glutathione reductase of Escherichia coli (1989)

Deonarain, M. P., Berry, A., Scrutton, N. S. & Perham, R. N.

Biochemistry, 28, 9602-9607, DOI: 10.1021/bi00451a008

[7] Switching kinetic mechanism and putative proton donor by directed mutagenesis of glutathione reductase (1989)

Berry, A., Scrutton, N. S. & Perham, R. N.

Biochemistry, 28, 1264-1269, DOI: 10.1021/bi00429a047

[6] NADPH generation in Aspergillus nidulans: is the mannitol cycle involved? (1988)

Singh, M., Scrutton, N. S. & Scrutton, M. C.

J. Gen. Microbiol., 134, 643-654, DOI: 10.1099/00221287-134-3-643 Free Access

[5] Engineering of an intersubunit disulphide bridge in glutathione reductase from Escherichia coli (1988)

Scrutton, N. S., Berry, A. & Perham, R. N.

FEBS Lett., 241, 46-50, DOI: 10.1016/0014-5793(88)81028-7 Free Access

[4] Flavoprotein disulphide oxidoreductases: protein engineering of glutathione reductase from Escherichia coli (1988)

Perham, R. N., Berry, A. & Scrutton, N. S.

Biochem. Soc. Trans., 16, 84-87, DOI: 10.1042/bst0160084

[2] Protein engineering of glutathione reductase from Escherichia coli (1987)

Scrutton, N. S., Berry, A. & Perham, R. N.

Flavins and Flavoproteins; Proceedings of the Ninth International Symposiym, Atlanta, Georgia, USA (Eds. D. E. Edmondson & D. B. McCormick) Walter de Gruyter & Co., Berlin. N.Y. pp. 85-88

[1] Protein engineering of glutathione reductase: overexpression of the gene from Escherichia coli (1986)

Scrutton, N. S., Berry, A. & Perham, R. N.

Biochem. Soc. Trans., 14, 1229-1230, DOI: 10.1042/bst0141229