Em Prof P M Harrison
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| Structure and structure-function relationships in metalloproteins, especially in the four-helix bundle dimetal proteins, ferritin and dimanganese catalase. Our X-ray crystallographic, spectroscopic and kinetic studies of ferritins from a wide variety of organisms have indicated that the first step in iron storage in ferritin is the catalytic oxidation of two Fe2+ by dioxygen at a dinuclear site. The mechanism of this and subsequent stages in iron storage are under intense investigation in our laboratory. In contrast to ferritin, the non-haem dimanganese catalase catalyses the dismutation of peroxide to dioxygen and water, but the two active sites are structurally similar. Structure-function comparisons are aimed at illuminating catalytic mechanisms in the two proteins. Collaboration with P J Artymiuk, J R Guest, V Barynin and others has been important for these interdisplinary studies. |
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Figure Legend - E. coli ferritin molecules in crystal. |
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Selected Publications
Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution. P.D.Hempstead, S.J. Yewdall, A.R. Fernie, D.M. Lawson, P.J. Artymiuk, D.W. Rice, G.C. Ford and P.M. Harrison. J.Mol.Biol. (1997), 268 424-448. |
| Solving the structure of human H-ferritin by genetically engineering intermolecular crystal contacts. D.M. Lawson, P.J. Artymiuk, S.J. Yewdall, J.M.A. Smith, J.C. Livingstone, A. Treffry, A. Luzzago, S. Levi, P. Arosio, G. Cesareni, C.D. Thomas, W.V. Shaw and P.M. Harrison. Nature (1991), 349, 541-544. |
| Ferritins - molecular properties, iron storage function and cellular regulation. P.M.Harrison and P. Arosio, BBA (1996) 1275, 161-203. |
| Dinuclear center of ferritin: studies of iron binding and oxidation show differences in the two iron sites. A.Treffry, Z. Zhao, M.A. Quail, J.R. Guest, P.M. Harrison. Biochem (1997) 36, 432-441. |
| V.Barynin et al, J.Inorg.Biochem (1997) |
