Murphy, Loretta M - Bangor University

个人简介

My current research programmes focus on the chemistry of metals in biological systems that have clinical and environmental relevance. If you wish to book an appointment, please do so through my ‘youcanbookme’ page. Bioinorganic chemistry is of fundamental importance to increasing our understanding of biological systems as approximately 30% of proteins in known genomes contain metal ions. Metalloproteins exploit the chemistry of metals and utilise this widely in many biological processes including respiration, photosynthesis, nitrogen fixation and protection against toxic agents. My current research programs focus on the chemistry of metals in biological systems that have clinical and environmental relevance. The majority of my research is multidisciplinary and utilises standard laboratory methods* for protein production/characterisation together with advanced synchrotron radiation techniques#. * chromatography, electrophoresis, electron paramagnetic spectroscopy, UV/Vis spectroscopy, atomic absorption spectroscopy, #X-ray absorption spectroscopy, protein crystallography, solution x-ray scattering.

研究领域

Bacterial Cytochromes c' are an interesting class of metalloproteins whose physiological role is yet to be clearly established. They are found in photosynthetic, nitrogen fixing and denitrifying bacteria. In denitrifying bacteria the role of Cyt c' has been postulated as mediating the toxicity of nitric oxide. This project is focused on the production and characterisation of site directed mutants of Cyt c' from Alcaligenes xylosoxidans in order to better understand this proteins role in denitrification – (collaboration with Prof. G. Sawyer (Martin-Luther University Halle-Wittenberg)Prof. S. Hasnain & Prof. R. Eady (Daresbury Laboratory) Pseudomonas aeruginosa is a Gram-negative bacterium of increasing clinical relevance as an opportunist pathogen of immunocompromised individuals, in particular burns and cystic fibrosis patients in which persistent Pseudomonas infection is a leading cause of mortality. LasA is a zinc-dependent protease that has been implicated in establishing Pseudomonas infection. However there is little structural or mechanistic information on this protein. Future experiments are aimed at establishing the likely catalytic mechanism, substrate specificity and role in Pseudomonas infection.- (collaboration with Dr J. Spencer, Bristol University) Acyl-activating enzyme 7 (AAE7 ) from Arabidopisis thaliana is a peroxisomal enzyme responsible for the activation of exogenous acetate to acetyl-coenzyme A for entry into the glyoxylate cycle. In order to better understand the nature of acetate metabolism in plants we have undertaken to elucidate the crystal and solution structure of AAE7 with and without substrate analogues (collaboration with Dr M. Hooks and Dr P. Murphy, Bangor University)

近期论文

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Modulation of NO binding to cytochrome c ' by distal and proximal haem pocket residues Barbieri S, Murphy LM, Sawers RG, Eady RR, Hasnain SS Journal of Biological Inorganic Chemistry, 2008, 13(4), 531-540. “Zn-Link": A metal-sharing interface that organizes the quaternary structure and catalytic site of the endoribonuclease, RNase E. Callaghan AJ, Redko Y, Murphy LM, Grossmann JG, Yates D, Garman E, Ilag LL, Robinson CV, Symmons MF, McDowall KJ, Luisi BF. Biochemistry, 2005, 44, No 12. pp 4667-4675. Experimental aspects of biological X-ray absorption Spectroscopy I. Ascone, W. Meyer-Klauke and L. Murphy Journal of Synchrotron Radiation, 2003, 10, 16-22 Electron Donation Between Copper Containing Nitrite Reductases and Cupredoxins: the Nature of Protein-protein Interaction in Complex Formation. L. M. Murphy, F. E. Dodd, F. K. Yousafzai, R. R. Eady and S. S. Hasnain Journal of Molecular Biology, 2002, 315 (4), 859-871 XAFS study of the high-affinity copper-binding site of human PrP91-231 and its low-resolution structure in solution S. S. Hasnain, L. M. Murphy, R. W. Strange, J. G. Grossmann, A. R. Clarke, G. S. Jackson and Collinge. Journal of Molecular Biology, 2001, 311, No 3, pp 467-473 Structural and kinetic evidence for an ordered mechanism copper nitrite reductase R. W. Strange, L.M. Murphy, F.E. Dodd, Z.H.L. Abraham, R.R. Eady, B.E. Smith and S.S. Hasnain Journal of Molecular Biology, 1999, 287 (5), 1001-1009