Peter Moody studied biochemistry at the University of York, where he worked on the structure of barnase with Guy & Eleanor Dodson and he was awarded the Ph.D. degree in biophysics from Imperial College in 1984, where he studied the structure and function of glyceraldehyde-3-phosphate dehydrogenase with Alan Wonacott in David Blow’s group. His postdoctoral work has been at Harvard with W.N. Lipscomp Jnr., at Imperial with Andrew Leslie and in York with Guy Dodson. Amongst the structures he has solved have been penicillin acylase (for which he proposed the “N-terminal nucleophile” mechanism), the suicidal DNA repair protein (O6alkylguanine-DNA alkyltransferase), the flavoenzymes PETN reductase & morphinone reductase & serine acetyl transferase. His current research interests include the structure and mechanisms of heme redox enzymes and of glycolytic enzymes from pathogens. He took his current post at the University of Leicester in 1995, where he sat up the protein crystallography laboratory. He has been a member of the Council of the British Crystallographic Association and is currently the Synchrotron Radiation User Group representative of the UK protein crystallography community. To date he has over 50 papers that have been cited over 2000 times.
Biography Updated on 20 November 2007