Colin Jackson

Group membership

Group Leader, Jackson Group - SynBio

Prof. Colin Jackson has held research positions at the Commonwealth Scientific and Industrial Research Organisation (CSIRO) and was a visiting research fellow at the Weizmann Institute of Science (Rehovot, Israel) and a Marie Curie Research Fellow at the Institut de Biologie Structurale (Grenoble, France), before his appointment as a Senior Lecturer at the Research School of Chemistry.

Research interests

Our research interests lie at the interface between biology, chemistry and physics and are directed towards gaining an understanding of the fundamental chemistry that underlies biological function. For example, how is an enzyme is capable of accelerating chemical reactions? Or, how do mutations allow enzymes to evolve new functions? Our group is also interested in applied science and using chemical techniques to manipulate biological systems, which can include the design of small molecules (drugs) that change the function of biological molecules or engineering proteins to make them function according to our needs.

  • Ney, B, Ahmed, H, Carere, C et al. 2017, 'The methanogenic redox cofactor F420 is widely synthesized by aerobic soil bacteria', The International Society of Microbial Ecology, vol. 11, no. 1, pp. 125-137pp.
  • Ney, B*, Ahmed, FH*, Carere, C et al 2017, 'The methanogenic redox cofactor F420 is widely synthesized by aerobic soil bacteria', The International Society of Microbial Ecology, vol. 11, no. 1, pp. 125-137pp. [*: joint first authors]
  • Mabbitt, P, Correy, G, Fraser, N et al. 2016, 'Conformational Disorganization within the Active Site of a Recently Evolved Organophosphate Hydrolase Limits Its Catalytic Efficiency', Biochemistry, vol. 55, no. 9, pp. 1408-1417.
  • Greening, C, Biswas, A, Carere, C et al 2016, 'Genomic and metagenomic surveys of hydrogenase distribution indicate H-2 is a widely utilised energy source for microbial growth and survival', The International Society of Microbial Ecology, vol. 10, no. 3, pp. 761-777pp.
  • Fraser, N, Liu, J, Mabbitt, P et al 2016, 'Evolution of Protein Quaternary Structure in Response to Selective Pressure for Increased Thermostability', Journal of Molecular Biology, vol. 428, no. 11, pp. 2359-2371.
  • Horgan, C, Han, Y, Trueman, H et al 2016, 'Phosphorescent oxygen-sensing and singlet oxygen production by a biosynthetic silk', RSC Advances, vol. 6, no. 46, pp. 39530-39533.
  • Correy, G, Carr, P, Meirelles Betancur, T et al. 2016, 'Mapping the Accessible Conformational Landscape of an Insect Carboxylesterase Using Conformational Ensemble Analysis and Kinetic Crystallography', Structure, vol. 24, no. 6, pp. 977-987.
  • Chan, K, Mabbitt, P, Phua, S et al. 2016, 'Sensing and signaling of oxidative stress in chloroplasts by inactivation of the SAL1 phosphoadenosine phosphatase', PNAS - Proceedings of the National Academy of Sciences of the United States of America, vol. 113, no. 31, pp. E4567-E4576.
  • Greening, C, Ahmed, H, Mohamed, A et al. 2016, 'Physiology, Biochemistry, and Applications of F-420- and F-o-Dependent Redox Reactions', Microbiology and Molecular Biology Reviews, vol. 80, no. 2, pp. 451-493.
  • Mohamed, A, Ahmed, H, Sundaram, A et al. 2016, 'Protonation state of F420H2 in the prodrug-activating deazaflavin dependent nitroreductase (Ddn) from Mycobacterium tuberculosis', Molecular BioSystems, vol. 12, no. 4, pp. 1110-1113.
  • Clifton, B & Jackson, C 2016, 'Ancestral Protein Reconstruction Yields Insights into Adaptive Evolution of Binding Specificity in Solute-Binding Proteins', Cell Chemical Biology, vol. 23, no. 2, pp. 236-245.
  • Greening, C*, Ahmed, FH*, Mohamed, AE et al 2016, 'Physiology, biochemistry, and applications of F420- and Fo-dependent redox reactions', Microbiology and Molecular Biology Reviews, vol. 80, no. 2, pp. 451-493. [*: joint first authors]
  • Mohamed, AE, Ahmed, FH, Arulmozhiraja, S et al 2016, 'Protonation state of F420H2 in the prodrug-activating deazaflavin dependent nitroreductase (Ddn) from Mycobacterium tuberculosis', Molecular BioSystems, vol. 12, no. 4, pp. 1110-1113.
  • Sugrue, E, Fraser, N, Hopkins, D et al. 2015, 'Evolutionary Expansion of the Amidohydrolase Superfamily in Bacteria in Response to the Synthetic Compounds Molinate and Diuron', Applied and Environmental Microbiology, vol. 81, no. 7, pp. 2612-2624.
  • Kaltenbach, M, Jackson, C, Campbell, E et al 2015, 'Reverse evolution leads to genotypic incompatibility despite functional and active site convergence', eLife, vol. 4, pp. 1-20.
  • Van Benschoten, A, Afonine, P, Terwilliger, T et al 2015, 'Predicting X-ray diffuse scattering from translation-libration-screw structural ensembles', Acta Crystallographica Section D: Biological Crystallography, vol. 71, no. Pt 8, pp. 1657-1667.
  • Whitfield, J, Zhang, W, Herde, M et al 2015, 'Construction of a robust and sensitive arginine biosensor through ancestral protein reconstruction', Protein Science, vol. 24, no. 9, pp. 1412-1422.
  • Riley, B, Broendum, S, Reboul, C et al 2015, 'Dynamic Motion and Communication in the Streptococcal C1 Phage Lysin, PlyC', PLOS ONE (Public Library of Science), vol. 10, no. 10, pp. e0140219-e0140219.
  • Banwell, M, Buckler, J, Jackson, C et al 2015, 'Devising New Syntheses of the Alkaloid Galanthamine, a Potent and Clinically Deployed Inhibitor of Acetylcholine Esterase', Strategies and Tactics in Organic Synthesis, vol. 11, pp. 29-50.
  • Ahmed, FH, Carr, P, Lee, B et al 2015, 'Sequence-Structure-Function Classification of a Catalytically Diverse Oxidoreductase Superfamily in Mycobacteria', Journal of Molecular Biology, vol. 427, no. 22, pp. 3554-3571.
  • Jackson, C, Carville, A, Ward, J et al 2014, 'Use of OpdA, an organophosphorus (OP) hydrolase, prevents lethality in an African green monkey model of acute OP poisoning', Toxicology, vol. 317, pp. 1-5.
  • Naqvi, T, Warden, A, French, N et al. 2014, 'A 5000-fold increase in the specificity of a bacterial phosphotriesterase for malathion through combinatorial active site mutagenesis', PLOS ONE (Public Library of Science), vol. 9, no. 4, pp. e94177-e94177.
  • Jackson, C, Coppin, C, Carr, P et al. 2014, '300-Fold Increase in Production of the Zn2+ -Dependent Dechlorinase TrzN in Soluble Form via Apoenzyme Stabilization', Applied and Environmental Microbiology, vol. 80, no. 13, pp. 4003-4011.
  • Lan, P, Jackson, C, Banwell, M et al 2014, 'Synthesis of a D-ring isomer of galanthamine via a radical-based Smiles rearrangement reaction', Journal of Organic Chemistry, vol. 79, no. 14, pp. 6759-6764.
  • Carr, P, Ewens, C, Dai, J et al. 2014, 'Crystal structure of the mouse interleukin-3 β-receptor: insights into interleukin-3 binding and receptor activation', Biochemical Journal, vol. 463, no. 3, pp. 393-403.
  • Tokuriki, N & Jackson, C 2014, 'Enzyme dynamics and engineering: one step at a time', Chemistry and Biology, vol. 21, no. 10, pp. 1259-1260.
  • Carruthers, T, Carr, P, Loh, C et al 2014, 'Iron(III) located in the dinuclear metallo-beta-lactamase IMP-1 by pseudocontact shifts', Angewandte Chemie International Edition, vol. 53, no. 51, pp. 14269-14272.
  • Jackson, C, Liu, J, Carr, P et al. 2013, 'Structure and function of an insect α-carboxylesterase (αEsterase7) associated with insecticide resistance', PNAS - Proceedings of the National Academy of Sciences of the United States of America, vol. 110, no. 25, pp. 10177-10182.
  • Zhang, W, Otting, G & Jackson, C 2013, 'Protein engineering with unnatural amino acids', Current Opinion in Structural Biology, vol. 23, no. 4, pp. 581-587.
  • Noor, S, Taylor, M, Russell, R et al 2012, 'Intramolecular epistasis and the evolution of a new enzymatic function', PLOS ONE (Public Library of Science), vol. 7, no. 6, pp. e39822-e39822.
  • Perriman, A, Weik, M, Gallat, F et al 2012, 'A polymer surfactant corona dynamically replaces water in solvent-free protein liquids and ensures macromolecular flexibility and activity', Journal of the American Chemical Society, vol. 134, no. 32, pp. 13168-13171.
  • Afriat-Jurnou, L, Jackson, C & Tawfik, D 2012, 'Reconstructing a missing Link in the Evolution of a Recently Diverged Phosphotriesterase by Active-Site Loop Remodeling', Biochemistry, vol. 51, no. 31, pp. 6047-6055.
  • Tokuriki, N, Jackson, C, Afriat-Jurnou, L et al 2012, 'Diminishing returns and tradeoffs constrain the laboratory optimization of an enzyme', Nature Communications, vol. 3, no. 12, pp. 1257-1257.
  • Coppin, C, Jackson, C, Sutherland, T et al 2012, 'Testing the evolvability of an insect carboxylesterase for the detoxification of synthetic pyrethroid insecticides', Insect Biochemistry and Molecular Biology, vol. 42, no. 5, pp. 343-352.
  • Russell, R, Scott, C, Jackson, C et al 2011, 'The evolution of new enzyme function: lessons from xenobiotic metabolizing bacteria versus insecticide-resistant insects', Evolutionary Applications, vol. 4, no. 2, pp. 225-248.
  • Ugwumba, I, Ozawa, K, Xu, Z et al. 2011, 'Improving a natural enzyme activity through incorporation of unnatural amino acids', Journal of the American Chemical Society, vol. 133, no. 2, pp. 326-333.
  • Brittain, D, Pandey, R, Kumari, K et al 2011, 'Competing SN2 and E2 reaction pathways for hexachlorocyclohexane degradation in the gas phase, solution and enzymes', Chemical Communications, vol. 47, no. 3, pp. 976-978.
  • Fraser, J & Jackson, C 2011, 'Mining electron density for functionally relevant protein polysterism in crystal structures', Cellular and Molecular Life Sciences, vol. 68, no. 11, pp. 1829-1841.
  • Sharma, P, Pandey, R, Kumari, K et al 2011, 'Kinetic and Sequence-Structure-Function Analysis of Known LinA Variants with Different Hexachlorocyclohexane Isomers', PLOS ONE (Public Library of Science), vol. 6, no. 9, pp. e25128-e25128.
  • Taylor, M, Jackson, C, Tattersall, D et al 2010, 'Identification and characterization of two families of F420H2-dependent reductases from Mycobacteria that catalyze aflatoxin degradation', Molecular Microbiology, vol. 78, no. 3, pp. 561-575.
  • Khersonsky, O, Rothlisberger, D, Dym, O et al 2010, 'Evolutionary optimization of computationally designed enzymes: Kemp eliminases of the KE07 series', Journal of Molecular Biology, vol. 396, no. 4, pp. 1025-1042.
  • Jackson, C, Gillam, E & Ollis, D 2010, 'Directed evolution of enzymes', in Lew Mander and Hung-Wen (Ben) Liu (ed.), Comprehensive Natural Products Chemistry II: Chemistry and Biology, Elsevier, Oxford, pp. 723-749.
  • Jackson, C, Oakeshott, J, Sanchez-Hernadez, J et al 2010, 'Caboxylesterases in the metabolism and toxicity of pesticides', in Satoh T., Gupta R.C. (ed.), Anticholinesterase Pesticides: Metabolism, Neurotoxicity, and Epidemiology, John Wiley & Sons Inc, Hoboken USA, pp. 57-75.
  • Lal, R, Pandey, G, Sharma, P et al 2010, 'Biochemistry of microbial degradation of hexachlorocyclohexane and prospects for bioremediation', Microbiology and Molecular Biology Reviews, vol. 74, no. 1, pp. 58-80.
  • Gresham, C, Rosenbaum, C, Gaspari, R et al 2010, 'Kinetics and efficacy of an organophosphorus hydrolase in a rodent model of methyl-parathion poisoning', Academic Emergency Medicine, vol. 17, no. 7, pp. 736-740.
  • Scott, C, Russell, R, Coppin, C et al 2010, Enzymes and methods for degrading S-triazines and diazines.
  • Khurana, J, Jackson, C, Scott, C et al 2010, Enzymes and methods for hydrolysing a phenylureas, carbamates and organophosphates.
  • Scott, C, Jackson, C, Coppin, C et al 2009, 'Catalytic improvement and evolution of atrazine chlorohydrolase', Applied and Environmental Microbiology, vol. 75, no. 7, pp. 2184-2191.
  • Scott, C, Jackson, C, Russell, R et al 2009, Enzymes and methods for degrading chlorinated S-triazines.
  • Weston, D & Jackson, C 2009, 'Use of engineered enzymes to identify organophosphate and pyrethroid-related toxicity in toxicity identification evaluations', Environmental Science and Technology, vol. 43, no. 14, pp. 5514-5520.
  • Scott, C, Pandey, G, Hartley, C et al 2008, 'The enzymatic basis for pesticide bioremediation', Indian Journal of Microbiology, vol. 48, no. 1, pp. 65-79.
  • Jackson, C, Hadler, K, Carr, P et al. 2008, 'Malonate-bound structure of the glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) and characterization of the native Fe2+ metal-ion preference', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 64, no. 8, pp. 681-685.
  • Hadler, K, Tanifum, E, Yip, S et al. 2008, 'Substrate-promoted formation of a catalytically competent binuclear center and regulation of reactivity in a glycerophosphodiesterase from Enterobacter aerogenes', Journal of the American Chemical Society, vol. 130, no. 43, pp. 14129-14138.
  • Jackson, C, Foo, J, Kim, H et al. 2008, 'In crystallo capture of a Michaelis complex and product-binding modes of a bacterial phosphotriesterase*', Journal of Molecular Biology, vol. 375, no. 5, pp. 1189-1196.
  • Jackson, C, Carr, P, Liu, J et al. 2007, 'The structure and function of a novel glycerophosphodiesterase from Enterobacter aerogenes', Journal of Molecular Biology, vol. 367, no. 4, pp. 1047-1062.
  • Ely, F, Foo, J, Jackson, C et al 2007, 'Enzymatic bioremediation: organophosphate degradation by binuclear metallo-hydrolases', Current Topics in Biochemical Research, vol. 9, no. 2, pp. 63-78.
  • Jackson, C, Carr, P, Kim, H et al. 2006, 'Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: the prominent role of iron in the heterobinuclear active site', Biochemical Journal, vol. 397, no. 3, pp. 501-508.
  • Jackson, C, Carr, P, Kim, H et al. 2006, 'The purification, crystallization and preliminary diffraction of a glycerophosphodiesterase from Enterobacter aerogenes', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 62, no. 7, pp. 659-661.
  • Yu McLoughlin, S, Jackson, C, Liu, J et al 2005, 'Increased expression of a bacterial phosphotriesterase in Escherichia coli through directed evolution', Protein Expression and Purification, vol. 41, no. 2, pp. 433-440.
  • Jackson, C, Kim, H, Carr, P et al. 2005, 'The structure of an enzyme-product complex reveals the critical role of a terminal hydroxide nucleophile in the bacterial phosphotriesterase mechanism', Biochimica et Biophysica Acta: International journal of Biochemistry and Biophysics, vol. 1752, no. 1, pp. 56-64.
  • Jackson, C, Liu, J, Coote, M et al 2005, 'The effects of substrate orientation on the mechanism of a phosphotriesterase', Organic and Biomolecular Chemistry, vol. 3, no. 24, pp. 4343-4350.
  • Yu McLoughlin, S, Jackson, C, Liu, J et al 2004, 'Growth of Escherichia coli coexpressing phosphotriesterase and glycerophosphodiester phosphodiesterase, using paraoxon as the sole phosphorus source', Applied and Environmental Microbiology, vol. 70, no. 1, pp. 404-412.