Emeritus Professor of Biology and Chemistry
Andrew Thomson’s major research interests throughout his career at UEA as founder Director of the Centre for Metalloprotein Spectroscopy and Biology, (CMSB) have been in the application of optical and magnetic methods to analyse the structures and functions of transition metal centres in proteins. Magnetic circular dichroism (MCD) and electron paramagnetic resonance (EPR) spectroscopy as well as novel optical-microwave double resonance techniques have been developed. The systems studied include enzymes of the bacterial denitrification pathway that contain hemoproteins, iron-sulfur and multi-copper clusters as well terminal heme-copper oxidases. proteins of iron uptake and storage pathways and proteins that utilise iron sulphur clusters to regulate gene expression. In 2005 Andrew Thomson established the Henry Wellcome Unit for Biological EPR Spectroscopy (Director Dr Fraser MacMillan) at UEA utilizing multi-frequency (9 and 95 GHz) and time domain EPR to map membrane metalloproteins using site directed spin labelling.
Early in his career after completing his PhD degree with RJP Williams in Oxford Andrew Thomson worked in the laboratory of B Rosenberg, between 1965-67, on the effect of platinum salts on bacterial growth processes. He was the first to show that the cis isomer of dichlorodiammineplatinum(II) (cisPlatin) was the effective biological agent in inhibiting cell divsion in E.coli. This led ultimatley to its clinical use as a highly effective chemotherapeutic agent against several cancers particularly testicular cancer.
Analysis of nitroxide spin label motions in a protein-protein complex using multiple frequency EPR spectroscopy.
Gaye F White, Louise Ottignon, Toni Georgiou, Colin Kleanthous, Geoff R Moore Andrew J Thomson, Vasily S Oganesyan.
J. Mag. Res. 2007 185, 191-203.
DOI: 10.1016/j.jmr.2006.12.009
Superoxide mediated-amplification of the oxygen-induced switch from [4Fe-4S] to [2Fe-2S] clusters in the transcriptional regulator FNR.
Jason C. Crack, Jeffrey Green, Myles R. Cheesman, Nick E. Le Brun and Andrew J. Thomson.
Proc. Natl. Acad. Sci. USA 2007 104, 2092-2097.
DOI:10.1073/pnas.0609514104
Magnetic circular dichroism anisotropy of the CuA centre of nitrous oxide reductase from coherent Raman detected electron spin resonance spectroscopy.
Stephen J Bingham, Tim Rasmussen, Jaqui Farrar, Daniel Wolverson, Andrew J. Thomson.
Molecular Physics 2007 105, 2169 - 2176.
DOI: 10.1080/00268970701732985
Influence of the Environment on the [4Fe-4S]2+ to [2Fe-2S]2+ Cluster Switch in the Transcriptional Regulator FNR.
Jason C. Crack, Jeffrey Green, Myles R. Cheesman, Nick E. Le Brun, and Andrew J. Thomson
J. Am. Chem. Soc. 2008 130 1749 – 1758.
DOI: 10.1021/ja077455+
Magnetic Circular Dichroism Spectroscopy of Antiferromagnetically Coupled Hetero-Metallic Rings [H2NR2][Cr7MF8(O2CCMe3)16].
Justin M. Bradley, Andrew J. Thomson, Eric J. McInnes, Richard E.P. Winpenny, Grigore Timco.
Dalton Trans. 2008 3311-3319
DOI: 10.1039/b803269f
Mitigating release of the potent greenhouse gas N2O from the nitrogen cycle – could enzymic regulation hold the key?
David Richardson, Heather Felgate, Nick Watmough, Andrew Thomson and Elizabeth Baggs.
Trends Biotechnol. 2009 27, 385-442
Optimizing the sensitivity to O2 of the transcription factor FNR: Ser24 modulates the kinetics of the [4Fe-4S] to [2Fe-2S] conversion.
AJ Jervis, JC Crack, G White, PJ Artymiuk, MR Cheesman, AJ Thomson, NE Le Brun, J Green.
Proc. Natl. Acad. Sci. USA. 2009 106, 4659-64
Wellcome Trust Witnesses to Twentieth Century Medicine Volume 30. “The Discovery, Use and Impact of Platinum Salts as Chemotherapy Agent for Cancer”.
Ed. DA Christie, EM Tansey.
Wellcome Trust Centre for the History of Medicine. UCL, 2007. ISBN 978 085484 112 7.
Pp 6-15 Contribution from Andrew J Thomson
Subunit Organization in the TatA Complex of the Twin Arginine Protein Translocase. A site-directed EPR spin labeling study.
Gaye F. White, Sonya M. Schermann, Justin Bradley, Andrew Roberts, Nicholas P. Greene, Ben C. Berks, and Andrew J. Thomson.
J. Biol Chem 2010 285 (no. 4) 2294 - 2301
DOI: 10.1074/jbc.M109.065458
ID: 24250