Biography

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Myles Cheesman graduated from University of Cambridge with a B.A. in Natural Sciences in 1983. He then moved to UEA to join the group of Professor Andrew Thomson and studied for a PhD on the spectroscopic properties of nickel ions and iron-sulphur clusters in bacterial proteins. Post-doctoral research on heme-copper oxidases was followed by a period as Senior Research Officer responsible for the Magnetic Circular Dichroism (MCD) and Electron Paramagnetic Resonance (EPR) laboratories of the Centre for Metalloprotein Spectroscopy and Biology (CMSB) and then appointment to faculty in 2004.

Myles’ research centres on the use of of MCD and EPR spectroscopy to study proteins containing transition metal ions:

One third of all proteins would not function were it not for the presence of one or more metal cofactors. Enzymes which catalyse the redox transformation of small inorganic substrates, such as O2, NO, NO2- and S2O32-, invariably contain transition metal ions, both as electron transfer centres and at the active site itself. Thus the bacterial enzymes which drive the global nitrogen and sulphur cycles and the enzymes of the O2-terminated respiratory chains of many organisms are almost all transition metalloproteins.

The techniques of MCD and EPR detect species which possess colour and paramagnetism and are therefore eminently suited to the study of these protein-bound inorganic complexes, providing information on metal identity, redox state, nature of ligands and interactions with other adjacent metal sites. These methods are currently used to study a wide variety of metalloproteins with a current emphasis on multiheme enzymes. Much of this work necessitates active collaboration with other research groups within the Henry Wellcome Laboratories for Biological Chemistry and with members of the School of Biological Sciences through the Centre for Metalloprotein Spectroscopy and Biology (CMSB).

Selected Publications

R.S. Pitcher, M.R. Cheesman and N.J.Watmough.
Molecular and spectroscopic analysis of the cytochrome cbb3 oxidase from Pseudomonas stutzeri
J. Biol. Chem., 2002, 277, 31474 – 31483.
DOI: 10.1074/jbc.M204103200

R.S. Zajicek, M.R. Cheesman, E.H.J. Gordon and S.J. Ferguson.
Y25S Variant of Paracoccus pantotrophus Cytochrome cd1 Provides Insight into Anion Binding by d1 Heme and a Rare Example of a Critical Difference between Solution of Crystal Structures
J. Biol Chem., 2005, 280, 26073-26079.
DOI: 10.1074/jbc.M501890200

S.J. Field, L. Prior, M.D. Roldan, M.R. Cheesman, A.J. Thomson, S. Spiro, J.N. Butt, N.J. Watmough and D.J. Richardson.
Spectral properties of bacterial nitric-oxide reductase - Resolution of pH-dependent forms of the active site heme b3
J. Biol. Chem., 2002, 277, 20146 – 20150.
DOI: 10.1074/jbc.M112202200

M.R. Cheesman, P.J. Little, and B.C. Berks.
Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum
Biochemistry, 2001, 40, 10562 – 10569.
DOI: 10.1021/bi0100081

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