- Grigg, J.C., Ukpabi, G., Gaudin, C.F.M & Murphy, M.E.P. (2009) Structural biology of heme binding in the Staphylococcus aureus Isd system. J. Inorg. Biochem. In press.
- Wong, S.G., Tom-Yew, S.A.L., Lewin, A.C., Le Brun, N., Moore, G.R., Murphy, M.E.P. & Mauk, A.G. (2009) Structural and mechanistic studies of a stabilized subunit dimer variant of Escherichia coli bacterioferritin identify residues required for core formation. J. Biol. Chem. 284, 18873-81.
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- Freeman, J.O., Lee, W.C., Murphy, M.E.P. & Sherman, J.C. (2009) X-ray crystal analysis of a TASP: structural insights of a cavitein dimer. J. Amer. Chem. Soc. 131, 7421-9.
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- Marchetti, A., Parker, M.S., Moccia, L.P., Lin, E.O., Arrieta, A.L., Murphy, M.E.P., Maldonado, M.T. & Armbrust, E.V. (2009) Ferritin is used for iron storage in bloom-forming marine pennate diatoms. Nature 457, 467-470.
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- Lee, W.C., Reniere, M.L., Skaar, E.P. & Murphy, M.E.P. (2008) Ruffling of metalloporphyrins bound to IsdG and IsdI, two heme degrading enzymes in Staphylococcus aureus. J. Biol. Chem. 283, 30957-63.
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- Tocheva, E.I., Eltis, L.D. & Murphy, M.E.P. (2008) Conserved active site residues limit inhibition of a copper-containing nitrite reductase by small molecules. Biochemistry 47, 4452-60.
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- Tocheva, E.I., Rosell, F.I., Mauk, A.G. & Murphy, M.E.P. (2007) Stable copper-nitrosyl formation by nitrite reductase in either oxidation state. Biochemistry 46, 12366-74.
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- Grigg, J.C., Vermeiren, C., Heinrichs, D.E., & Murphy, M.E.P. (2007) Heme coordination by Staphylococcus aureus IsdE. J. Biol. Chem. 282, 28815-22.
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- Wijma, H.J., MacPherson, I., Farver, O., Tocheva, E.I., Pecht, I., Verbeet, M.Ph., Murphy, M.E.P. Canters, G.W. (2007) Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite reductase. J. Amer. Chem. Soc. 129, 519-25.
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- MacPherson, I.S. & Murphy, M.E.P. (2007) Type 2 copper-containing enzymes. Cell. Mol. Life Sci. 64, 2887-2899.
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- Grigg, J.C., Vermeiren, C., Heinrichs, D.E., Murphy, M.E.P. (2007) Heme recognition by a Staphylococcus aureus NEAT domain. Mol. Microbiol. 63, 139-149.
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- Chan, A.C.K., Lelj-Garolla, B., Rosell, F.I., Pedersen, K.A., Mauk, A.G., and Murphy, M.E.P. (2006) Cofacial heme binding is linked to dimerization by a Campylobacter jejuni heme transport protein. J. Mol. Biol. 362, 1108-1119.
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- Tocheva, E.I., Fortin, P.D., Eltis, L.D., Murphy, M.E.P. (2006) Structures of ternary complexes of BphK, a bacterial GST that reductively dehalogenates PCB intermediates. J. Biol. Chem. 281, 30933-30940.
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- Tom-Yew, S.A.L., Cui, D.T., Bekker, E., and Murphy M.E.P. (2005) Iron coordination to the Campylobacter jejuni ferric binding protein is anion-independent. J. Biol. Chem. 280, 9283-90.
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- Tocheva, E. T., Rosell, F.I., Mauk, A.G. and Murphy, M.E.P. (2004). Side-on copper-nitrosyl coordination by nitrite reductase. Science 304, 867-870.
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- Bekker, E., Creagh, L., Sanaie, N, Yumoto, F., Lau, G.H.Y., Tanokura, M., Haynes, C. and Murphy, M.E.P. (2004). Specificity of the synergistic anion in ferric bind protein from Neisseria gonorrhoeae. Biochemistry, 43, 9195-9203.
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Last updated on August 18, 2010 @3:43 pm
