Professor Andrew Smith



School /
Work Unit

School of Science

Contact Details

No Phone


City campus


Science, Engineering and Health

Andrew T Smith


BSc and AUS (University of Surrey, UK)

PhD (University of Southampton, UK)

External & visiting appointments

Visiting Prof, Department of Chemistry and Biochemistry, School of Life Sciences, University of Sussex UK.

Affiliations / Professional memberships

Inorganic Biochemistry Discussion Group, Biochemical Society

Areas of research interests:

Structure/function relationships and mechanisms of metalloenzymes with particular emphasis on haem systems and peroxidases, particularly those that play a role in the degradation of lignin, the recalcitrant biopolymer that gives wood its strength. Degradation of lignin is known to be rate limiting in the carbon cycle and clean technologies that would help us unlock lignin and hence cellulose as renewable sources of chemicals and fuels may be of great importance in the future. Professor Smith’s research group is exploring the relatonships between globins, peroxidases and cytochromes P450 using horseradish peroxidase and lignin peroxidase as our main model systems. We are attempting to understand the structural determinants of activity and specificity with a view to creating new catalytic activities, such as the ability to fragment lignin (WO/2006/114616) or selectively oxygenate substrates (WO/2007/020428). The research is multidisciplinary in nature and at the interface between Chemistry and Biology. Recent highlights have included the structure of HRP in all five oxidation states (in collaboration with others) published in Nature (2002) and the role of a redox active Trp residue in the catalytic cycle of an engineered lignin peroxidase published in PNAS (2009).


Journal publications:

  1. Smith, A.T., Doyle, W.A., Dorlet, P. and Ivancich, A. (2009) Spectroscopic evidence for an engineered catalytically-active Trp radical that creates the unique reactivity of lignin peroxidase. PNAS 106, 1684-1689.
  2. Wiseman, B., Colin, J., Smith, A.T., Ivancich, A. and Loewen P.C. (2009) Mechanistic insight into the initiation step of the reaction of Burkholderia pseudomallei catalase-peroxidase with peroxyacetic acid. Journal of Biological Inorganic Chemistry, 14, 5, 801-811.
  3. Ruiz-Dueñas, F.J. , Morales, M., Mate, M.J. Romero, A., Martínez, M.J., Smith, A.T. and Martínez, A.T. (2008) Site-directed mutagenesis of the catalytic tryptophan environment in Pleurotus eryngii versatile peroxidase. Biochemistry, 47, 1685-1695.
  4. Smith A.T and Ngo E. (2007) Novel peroxidases and uses, Patent number: WO/2007/020428 PCT/GB2006/003045.
  5. Smith A.T. and Doyle W.A. (2006) Engineered peroxidases with veratryl alcohol oxidase activity, Patent number: WO/2006/114616, PCT/GB2006/001515.
  6. Howes, B. D., Brissett, N.C., Doyle, W.A, Smith, A.T & Smulevich, G. Spectroscopic and Kinetic Properties of the Horseradish Peroxidase Mutant T171S: Evidence for Selective Effects on the Reduced State of the Enzyme (2005) FEBS 272, 5514.
  7. O'Brien, A.M., Smith, A.T., O'Faigain, C. (2003) Effects of phthalic anhydride modification on horseradish peroxidase stability and activity. Biotech & Bioengineering 81, 233-240.
  8. Meno, K., Jennings, S., Smith, A.T., Henricksen, A, & Gajhede, M (2002) Structural analysis of the two horseradish peroxidase catalytic residue variants H42E and R38S:H42E: Implications for the catalytic cycle. Acta Cry. Sec. D - Biol. Cry. 58, 1803-12.
  9. Hiner A.N.P., Hermandez-Ruiz, J., Rodrigues Lopez, J.N., Garcia-Canovas, F., Brissett, N.C., Smith A.T., Arnao M.B., & Acosta, M. (2002) Reactions of the class II peroxidases, lignin peroxidase and Arthromyces ramosus peroxidase, with hydrogen peroxide - Catalase-like activity, compound III formation and enzyme inactiviation. J. Biol. Chem. 277, 26879-26885.
  10. Berglund, G.I., Carlsson, G.H., Smith, A.T. Szoke, H., Henriksen, A., & Hajdu, J. (2002) The catalytic pathway of horseradish peroxidase at high resolution. Nature 417, 463-468.
  11. Heering, H.A. Smith, A.T. & Smulevich. G. (2002) Spectroscopic characterisation of mutations at the Phe 41 position in the distal heme pocket of horseradish peroxidase C: Structural and functional consequences. Biochem. J. 363, 571-579.
  12. Adams, B., Lowe, D.J., Smith, A.T., Scazzocchio, C., Demais, S & Bray, R.C. (2002). Expression of Drosophila melanogaster xanthine dehydrogenase in Aspergillus nidulans and properties of the recombinant wild-type enzyme. Biochem. J. 362, 223-229.
  13. Perez-Boada, M., Doyle, W.A., Ruiz-Duenas, F.J., Martinez, M.J. Martinez, A.T & Smith A.T. (2002) Folding optimisation of Pleurotus eryngii versatile peroxidase expressed in E.Coli. Enz. Microbial. Tech. 30, 518-524.
  14. Heering H.A., Jansen M.A.K., Schneider-Belhaddad F., Smith A.T, Thorneley RNF, & Smulevich. G. (2001) Spectroscopic characterization of two atypical class III peroxidases from tea. J. Inorg. Biochem 86, (1): 256.
  15. Smith A.T. & Schneider-Belhaddad F. (2001) Mimicking the active site of chloroperoxidase: characterisation of the HRP distal pocket mutants R38H/H42E, R38H:F41A:H42E and R38A:F41H:H42E. J. Inorg. Biochem 86, (1): 99.
  16. Howes, B.D., Hendrik H.A. Roberts, T.O., Schneider-Belhaddad, F., Smith, A.T. & Smulevich, G. (2001) Mutation of residues critical for benzohydroxamic acid binding to horseradish peroxidase isoenzyme c. Biopolymers 62, 261-267.
  17. Coen, J.F., Smith, A.T., Candeias L.P. & Oakes, J. (2001) New insights into the mechanisms of dye degradation by one electron oxidation processes. J. Chem. Soc. Perkin Trans 2 2125-2129.
  18. Bray, R.C., Adams, B., Smith, A.T., Richards, R., Lowe, D.J. & Bailey. S. (2001) Reactions of dimethyl sulphoxide reductase in the presence of dimethylsulphide and the structure of the dimethylsulphide-modified enzyme. Biochemistry 40, 9810-9820.
  19. Piontek, K., Smith, A.T. & Blodig, W. (2001) Lignin peroxidase structure and function. Biochem. Soc. Trans 29, 111-115. (symposium paper).
  20. Howes, B. D., Veitch, N. C., Smith A. T, White, C.G & Smulevich. G. (2001). Haem-linked interactions in horseradish peroxidase revealed by spectroscopic analysis of the Phe-221-Met mutant. Biochem J. 353, 181-191.
  21. Blodig, W., Smith, A.T., Doyle, W.A & Piontek, K (2001). Crystal structures of pristine and oxidatively processed lignin peroxidase and the W171F mutant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism. J. Mol. Biol. 305, 851-861.
  22. Veitch, N.C & Smith, A.T (2001) Horseradish peroxidase Adv. in Inorg. Chemistry 51, 107-161.
  23. Bray, R.C, Adams, B., Smith, A.T., Bennett, B. &. Bailey, S. (2000) Reversible dissociation of thiolate ligands from molybdenum in an enzyme of the dimethyl sulfoxide reductase family. Biochemistry 39, 11258-11269.
  24. Henriksen, A., Smith, A.T., & Gajhede, M. (1999) The crystal structures of the horseradish peroxidase-ferulic acid complex and a ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates. J. Biol. Chem. 274, 35005-35011.
  25. Canne, C., Lowe, D.J., Fetzner, S., Adams, B., Smith, A.T., Kappl, R., Bray, R.C & Hüttermann, J. (1999) Kinetics and interactions of molybdenum and iron-sulfur centers in bacterial enzymes of the Xanthine Oxidase family: Mechanistic implications. Biochemistry 38, 14077-14087.
  26. Blodig W, Doyle W, Smith A.T, Winterhalter K, & Piontek K. (1999) The redox cycle of lignin peroxidase involves a transient tryptophan radical at the surface residue 171. J. Inorg. Biochem 74, 266-266.
  27. Heering, H.A., Smith, A.T. & Smulevich, G. (1999) Role of the distal Phe41 on the properties of horseradish peroxidase C, investigated by resonance Raman and electronic absorption spectroscopy. J. Inorg. Biochem 74, 157-157.
  28. Blodig, W., Smith, A.T., Winterhalter, K & Piontek, K. (1999) Trapping a transient radical on Trp171 of lignin peroxidase. Arch. Biochem. Biophy. 370, 86-92.
  29. Adams, B., Smith, A.T., Bailey, S., McEwan, A.G., & Bray, R.C. (1999) Reactions of dimethylsulphoxide reductase from Rhodobacter capsulatus with dimethyl sulphide and dimethylsulphoxide: complexities revealed by conventional and stopped-flow spectrophotometry. Biochemistry 38, 8501-8511.
  30. Doyle, W.A., Blodig, W., Veitch., N., Piontek, K., & Smith A.T. (1998) Two substrate interaction sites in lignin peroxidase revealed by site directed mutagenesis. Biochemistry 37, 15097-15105.
  31. Henriksen, A., Schuller, D.J., Meno, K., Welinder, K,G., Smith A.T & Gajhede, M. (1998) Structural interactions between horseradish peroxidase c and the substrate benzhydroxamic acid determined by X-ray crystallography at 2.0Å. Biochemistry 37, 8054-8060.
  32. Smith, A.T. & Veitch, N.C. (1998) Structural versatility of heme peroxidases for substrate binding and catalysis. An invited review for Curr. Opin. in Chem. Biol. 2, 269-278.
  33. Blodig, W., Doyle, W., Smith, A.T. & Piontek, K. (1998) Autocatalytic formation of a hydroxy group at Cb of Trp171 in lignin peroxidase. Biochemistry 37, 8832-8838.
  34. Meunier, B., Rodregez-Lopez, J.N., Thorneley., R.N.F., Smith, A.T. & Rich, P.R (1998). Redox- and anion-linked protonation sites in horseradish peroxidase: analysis of distal haem pocket mutants Biochem. J. 330, 303-309.
  35. Rasmussen, C.B., Hiner, A.N.P., Smith A.T. & Welinder, K.G. (1998) Effect of calcium, other ions, and pH on the reactions of barley peroxidase with hydrogen peroxide and fluoride. Control of activity through conformational change. J. Biol. Chem. 273, 2232-2240.
  36. Gajhede, M., Schuller, D.J., Henricksen, A., Smith., A.T & Poulos, T.L (1997) Crystal structure determination of classical horseradish peroxidase at 2.15Å resolution. Nature Structural Biology, 4 1032-1039.
  37. Veitch N.C., Gao Y., Smith A.T., & White C.G. (1997) Identification of a critical phenylalanine residue in horseradish peroxidase, Phe179, by site-directed mutagenesis and 1H-NMR: Implications for complex formation with aromatic donor molecules. Biochemistry 36, 14751-14761.
  38. Abelskov, A.K., Smith A.T., Rasmussen, C.B., Dunford, H.B & Welinder, K.G. (1997) pH-dependence and structural interpretation of the reactions of Coprinus cinereus peroxidase with hydrogen peroxide, ferulic acid and ABTS. Biochemistry 36, 9453-9463.
  39. Hill, A.P., Modi, S., Sutcliffe, M.J., Turner, D.D., Gilfoyle, D.J, Smith, A.T., Tam, B. & Lloyd, E. (1997) Chemical, spectroscopic and structural investigation of the substrate binding site in acorbate peroxidase. Eur. J. Biochem 248, 347-354.
  40. Howes, B.D., Rodreguez-Lopez, J.N., Smith, A.T.& Smulevich, G. (1997) Mutation of distal residues of horseradish peroxidase: Influence on substrate binding and cavity properties Biochemistry 36, 1532-1543.
  41. Rodregez-Lopez, J.N., Smith. A.T. & Thorneley, R.N.F. (1997) Effect of distal cavity mutations on the binding and activation of oxygen by ferrous horseradish peroxidase. J. Biol. Chem 272, 389-395.
  42. Doyle, W.A. & Smith, A.T. (1996) Expression of lignin peroxidase H8 in Escherichia coli: folding and activation of the recombinant enzyme with Ca2+ and heme. Biochem. J. 315, 15-19.
  43. Smith, A.T., Santama, N., Dacey, S., Edwards, M., Bray, R.C., Thorneley, R.N.F. & Burke, J.F. (1990) Expression of a Synthetic Gene for Horseradish Peroxidase C in Escherichia coli and Folding and Activation of the Recombinant Enzyme with Ca2+ and Heme. J. Biol. Chem. 265, 22, 13335-13343.