Professor Michael Wilson

Svistunenko, DA., Pullin, J., Bradley, J., Moore, G., Le Brun, N. and Wilson, M., (2021). Electron transfer from haem to the di‐iron ferroxidase centre in bacterioferritin. Angewandte Chemie International Edition. 60 (15), 8376-8379

Pullin, J., Wilson, MT., Clémancey, M., Blondin, G., Bradley, JM., Moore, GR., Le Brun, NE., Lučić, M., Worrall, JAR. and Svistunenko, DA., (2021). Iron oxidation in Escherichia coli bacterioferritin ferroxidase centre, a site designed to react rapidly with H2O2 but slowly with O2. Angewandte Chemie International Edition. 60 (15), 8361-8369

Lučić, M., Wilson, MT., Svistunenko, DA., Owen, RL., Hough, MA. and Worrall, JAR., (2021). Aspartate or arginine? Validated redox state X-ray structures elucidate mechanistic subtleties of FeIV = O formation in bacterial dye-decolorizing peroxidases. Journal of Biological Inorganic Chemistry. 26 (7), 743-761

Lucic, M., Chaplin, AK., Moreno-Chicano, T., Dworkowski, F., Wilson, M., Svistunenko, D., Hough, M. and Worrall, JAR., (2020). A subtle structural change in the distal haem pocket has a remarkable effect on tuning hydrogen peroxide reactivity in dye decolourising peroxidases from Streptomyces lividans. Dalton Transactions. 49 (5), 1620-1636

Straw, ML., Hough, MA., Wilson, MT. and Worrall, JAR., (2019). A histidine residue and a tetranuclear cuprous‐thiolate cluster dominate the copper loading landscape of a copper storage protein from Streptomyces lividans. Chemistry – A European Journal. 25 (45), 10678-10688

Deacon, OM., Svistunenko, DA., Moore, GR., Wilson, MT. and Worrall, JAR., (2018). Naturally Occurring Disease-Related Mutations in the 40–57 Ω-Loop of Human Cytochrome c Control Triggering of the Alkaline Isomerization. Biochemistry. 57 (29), 4276-4288

Welbourn, EM., Wilson, MT., Yusof, A., Metodiev, MV. and Cooper, CE., (2017). The mechanism of formation, structure and physiological relevance of covalent hemoglobin attachment to the erythrocyte membrane. Free Radical Biology and Medicine. 103, 95-106

Chaplin, AK., Svistunenko, DA., Hough, MA., Wilson, MT., Vijgenboom, E. and Worrall, JAR., (2017). Active site maturation and activity of the copper-radical oxidase GlxA is governed by a tryptophan residue. The Biochemical Journal. 474 (5), 809-825

Chaplin, AK., Wilson, MT. and Worrall, JAR., (2017). Kinetic characterisation of a dye decolourising peroxidase from Streptomyces lividans: New insight into the mechanism of anthraquinone dye decolourisation. Dalton Transactions. 46 (29), 9420-9429

Voong, CP., Spencer, PS., Navarrete, CV., Turner, D., Hayrabedyan, SB., Crummy, P., Holloway, E., Wilson, MT., Smith, PR. and Fernández, N., (2017). HLA-DR genotyping and mitochondrial DNA analysis reveal the presence of family burials in a fourth century Romano-British Christian cemetery. Frontiers in Genetics. 8 (DEC), 182-

Chaplin, AK., Wilson, MT., Hough, MA., Svistunenko, DA., Hemsworth, GR., Walton, PH., Vijgenboom, E. and Worrall, JAR., (2016). Heterogeneity in the Histidine-brace Copper Coordination Sphere in Auxiliary Activity Family 10 (AA10) Lytic Polysaccharide Monooxygenases. Journal of Biological Chemistry. 291 (24), 12838-12850

Karsisiotis, AI., Deacon, OM., Wilson, MT., Macdonald, C., Blumenschein, TMA., Moore, GR. and Worrall, JAR., (2016). Increased dynamics in the 40–57 Ω-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation. Scientific Reports. 6 (1), 30447-

Silkstone, G. and Wilson, MT., (2016). A Further Investigation of the Effects of Extremely Low Frequency Magnetic Fields on Alkaline Phosphatase and Acetylcholinesterase. PloS One. 11 (3), creators-Wilson=3AMichael_T=3A=3A

Manole, A., Kekilli, D., Svistunenko, DA., Wilson, MT., Dobbin, PS. and Hough, MA., (2015). Conformational control of the binding of diatomic gases to cytochrome c′. JBIC Journal of Biological Inorganic Chemistry. 20 (4), 675-686

Beckerson, P., Reeder, BJ. and Wilson, MT., (2015). Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding. FEBS Letters. 589 (4), 507-512

Porto, TV., Wilson, MT. and Worrall, JAR., (2015). Copper and nickel bind via two distinct kinetic mechanisms to a CsoR metalloregulator. Dalton Transactions. 44 (46), 20176-20185

Beckerson, P., Wilson, MT., Svistunenko, DA. and Reeder, BJ., (2015). Cytoglobin ligand binding regulated by changing haem-co-ordination in response to intramolecular disulfide bond formation and lipid interaction. Biochemical Journal. 465 (1), 127-137

Ghafoor, DD., Kekilli, D., Abdullah, GH., Dworkowski, FSN., Hassan, HG., Wilson, MT., Strange, RW. and Hough, MA., (2015). Hydrogen bonding of the dissociated histidine ligand is not required for formation of a proximal NO adduct in cytochrome c’. JBIC Journal of Biological Inorganic Chemistry. 20 (6), 949-956

Silaghi-Dumitrescu, R., Scurtu, F., Mason, MG., Svistunenko, DA., Wilson, MT. and Cooper, CE., (2015). The reaction of oxyhemoglobin with nitric oxide: EPR evidence for an iron(III)-nitrate intermediate. Inorganica Chimica Acta. 436, 179-183

Ascenzi, P., Coletta, M., Wilson, MT., Fiorucci, L., Marino, M., Polticelli, F., Sinibaldi, F. and Santucci, R., (2015). Cardiolipin-cytochromeccomplex: Switching cytochromecfrom an electron-transfer shuttle to a myoglobin- and a peroxidase-like heme-protein. IUBMB Life. 67 (2), 98-109

van Wilderen, LJGW., Silkstone, G., Mason, MG., van Thor, JJ. and Wilson, MT., (2015). Kinetic studies on the oxidation of semiquinone and hydroquinone forms of Arabidopsis cryptochrome by molecular oxygen. FEBS Open Bio. 5 (1), 885-892

Kassa, T., Jana, S., Strader, MB., Meng, F., Jia, Y., Wilson, MT. and Alayash, AI., (2015). Sickle cell hemoglobin in the ferryl state promotes ?Cys93 oxidation and mitochondrial dysfunction in epithelial lung cells (E10). The Journal of biological chemistry. 290 (46), 27939-27958

Hough, MA., Silkstone, G., Worrall, JAR. and Wilson, MT., (2014). NO Binding to the Proapoptotic Cytochrome c–Cardiolipin Complex. NITRIC OXIDE. 96, 193-209

Lobato, L., Bouzhir-Sima, L., Yamashita, T., Wilson, MT., Vos, MH. and Liebl, U., (2014). Dynamics of the Heme-binding Bacterial Gas-sensing Dissimilative Nitrate Respiration Regulator (DNR) and Activation Barriers for Ligand Binding and Escape. The Journal of biological chemistry. 289 (38), 26514-26524

Strader, MB., Hicks, WA., Kassa, T., Singleton, E., Soman, J., Olson, JS., Weiss, MJ., Mollan, TL., Wilson, MT. and Alayash, AI., (2014). Post-translational Transformation of Methionine to Aspartate Is Catalyzed by Heme Iron and Driven by Peroxide: A NOVEL SUBUNIT-SPECIFIC MECHANISM IN HEMOGLOBIN. The Journal of Biological Chemistry. 289 (32), 22342-22357

Ashe, D., Alleyne, T., Wilson, MT., Svistunenko, DA. and Nicholls, P., (2014). Redox equilibration after one-electron reduction of cytochrome c oxidase: Radical formation and a possible hydrogen relay mechanism. Archives of Biochemistry and Biophysics. 554, 36-43

Nicholls, P., Marshall, DCA., Cooper, CE. and Wilson, MT., (2014). Sulfide complex formation and redox interactions with heme enzymes. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1837, creators-Wilson=3AMichael_T=3A=3A

Cooper, CE., Schaer, DJ., Buehler, PW., Wilson, MT., Reeder, BJ., Silkstone, G., Svistunenko, DA., Bulow, L. and Alayash, AI., (2013). Haptoglobin Binding Stabilizes Hemoglobin Ferryl Iron and the Globin Radical on Tyrosine β145. Antioxidants & Redox Signaling. 18 (17), 2264-2273

Rong, Z., Alayash, AI., Wilson, MT. and Cooper, CE., (2013). Modulating hemoglobin nitrite reductase activity through allostery: A mathematical model. Nitric Oxide. 35, 193-198

Ascenzi, P., Marino, M., Polticelli, F., Coletta, M., Gioia, M., Marini, S., Pesce, A., Nardini, M., Bolognesi, M., Reeder, BJ. and Wilson, MT., (2013). Non-covalent and covalent modifications modulate the reactivity of monomeric mammalian globins. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1834 (9), 1750-1756

Nicholls, P., Marshall, DC., Cooper, CE. and Wilson, MT., (2013). Sulfide inhibition of and metabolism by cytochrome c oxidase. Biochemical Society Transactions. 41 (5), 1312-1316

Rong, Z., Wilson, MT. and Cooper, CE., (2013). A model for the nitric oxide producing nitrite reductase activity of hemoglobin as a function of oxygen saturation. Nitric Oxide. 33, 74-80

Blundell, KLIM., Wilson, MT., Svistunenko, DA., Vijgenboom, E. and Worrall, JAR., (2013). Morphological development and cytochrome c oxidase activity in Streptomyces lividans are dependent on the action of a copper bound Sco protein.. Open biology. 3 (1)

Blundell, KLIM., Wilson, MT., Vijgenboom, E. and Worrall, JAR., (2013). The role of the Cys-X-X-X-Cys motif on the kinetics of cupric ion loading to the Streptomyces lividans Sco protein. Dalton Transactions. 42 (29), creators-Wilson=3AMichael_T=3A=3A

Reeder, BJ., Svistunenko, DA., Cooper, CE. and Wilson, MT., (2012). Engineering Tyrosine-Based Electron Flow Pathways in Proteins: The Case of Aplysia Myoglobin. Journal of the American Chemical Society. 134 (18), 7741-7749

Rajagopal, BS., Silkstone, GG., Nicholls, P., Wilson, MT. and Worrall, JAR., (2012). An investigation into a cardiolipin acyl chain insertion site in cytochrome c. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817 (5), 780-791

Marshall, DCA., Nicholls, P., Wilson, MT. and Cooper, CE., (2012). A comparison of nitric oxide and hydrogen sulphide interactions with mitochondrial cytochrome c oxidase. Nitric Oxide: Biology and Chemistry. 27, S11-S12

Rong, Z., Wilson, MT. and Cooper, CE., (2012). A model of the NO producing nitrite reductase activity of hemoglobin. Nitric Oxide: Biology and Chemistry. 27, creators-Wilson=3AMichael_T=3A=3A

Reeder, BJ., Svistunenko, DA. and Wilson, MT., (2011). Lipid binding to cytoglobin leads to a change in haem co-ordination: a role for cytoglobin in lipid signalling of oxidative stress.. The Biochemical journal. 434 (3), 483-492

Rajagopal, BS., Wilson, MT., Bendall, DS., Howe, CJ. and Worrall, JAR., (2011). Structural and kinetic studies of imidazole binding to two members of the cytochrome c 6 family reveal an important role for a conserved heme pocket residue. JBIC Journal of Biological Inorganic Chemistry. 16 (4), 577-588

Boutaud, O., Moore, KP., Reeder, BJ., Harry, D., Howie, AJ., Wang, S., Carney, CK., Masterson, TS., Amin, T., Wright, DW., Wilson, MT., Oates, JA. and Roberts, LJ., (2010). Acetaminophen inhibits hemoprotein-catalyzed lipid peroxidation and attenuates rhabdomyolysis-induced renal failure. Proceedings of the National Academy of Sciences. 107 (6), 2699-2704

Cooper, CE., Holladay, R., Nicholls, P., Svistunenko, DA., Mason, MG., Silkstone, G. and Wilson, MT., (2010). Nitric Oxide Interactions With Mitochondrial Cytochrome C And Cytochrome Oxidase. Free Radical Biology And Medicine. 49 (1), creators-Wilson=3AMichael_T=3A=3A

Silkstone, G., Kapetanaki, SM., Husu, I., Vos, MH. and Wilson, MT., (2010). Nitric oxide binds to the proximal heme coordination site of the ferrocytochrome c/cardiolipin complex: formation mechanism and dynamics.. The Journal of biological chemistry. 285 (26), 19785-92

Godoy, LC., Munoz-Pinedo, C., Castro, L., Cardaci, S., Schonhoff, CM., King, M., Tortora, V., Marin, M., Miao, Q., Jiang, JF., Kapralov, A., Jemmerson, R., Silkstone, GG., Patel, JN., Evans, JE., Wilson, MT., Green, DR., Kagan, VE., Radi, R. and Mannick, JB., (2009). Disruption of the M80-Fe ligation stimulates the translocation of cytochrome c to the cytoplasm and nucleus in nonapoptotic cells. Proceedings Of The National Academy Of Sciences Of The United States Of America. 106 (8), 2653-2658

Reeder, BJ., Svistunenko, DA., Cooper, CE. and Wilson, MT., (2009). Engineering Electron Transfer Pathways in Myoglobin and Hemoglobin: A Route to Detoxify Blood Substitutes?. Free Radical Biology And Medicine. 47, creators-Wilson=3AMichael_T=3A=3A

Kapetanaki, SM., Silkstone, G., Husu, I., Liebl, U., Wilson, MT. and Vos, MH., (2009). Interaction of Carbon Monoxide with the Apoptosis-Inducing Cytochrome c-Cardiolipin Complex. Biochemistry. 48 (7), 1613-1619

Wilson, MT. and Reeder, BJ., (2008). Oxygen‐binding haem proteins. Experimental Physiology. 93 (1), 128-132

Reeder, BJ., Hider, RC. and Wilson, MT., (2008). Iron chelators can protect against oxidative stress through ferryl heme reduction. Free Radical Biology and Medicine. 44 (3), 264-273

Reeder, BJ., Cutruzzola, F., Bigotti, MG., Hider, RC. and Wilson, MT., (2008). Tyrosine as a redox-active center in electron transfer to ferryl heme in globins. Free Radical Biology and Medicine. 44 (3), 274-283

Reeder, BJ., Grey, M., Silaghi-Dumitrescu, R-L., Svistunenko, DA., Bülow, L., Cooper, CE. and Wilson, MT., (2008). Tyrosine Residues as Redox Cofactors in Human Hemoglobin. Journal of Biological Chemistry. 283 (45), 30780-30787

Cooper, CE., Silkstone, G., Mason, MG., Nicholls, P. and Wilson, MT., (2008). Interactions of nitric oxide with cytochrome c and cytochrome c oxidase. Biochimica et Biophysica Acta: Bioenergetics. 1777, S57-S58

Wilson, MT., (2008). Introduction: Andrew Thomson and the Centre for Metalloprotein Spectroscopy and Biology at the University of East Anglia. Biochemical Society Transactions. 36 (6), 1103-1105

Flors, C., (2006). Imaging the production of singlet oxygen in vivo using a new fluorescent sensor, Singlet Oxygen Sensor Green(R). Journal of Experimental Botany. 57 (8), 1725-1734