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Adams, Hannah R and Svistunenko, Dimitri A and Wilson, Michael T and Fujii, Sotaro and Strange, Richard W and Hardy, Zoe A and Vazquez, Priscilla A and Dabritz, Tyler and Streblow, Gabriel J and Andrew, Colin R and Hough, Michael A (2023) A heme pocket aromatic quadrupole modulates gas binding to cytochrome c'-β: Implications for NO sensors. Journal of Biological Chemistry, 299 (6). p. 104742. DOI https://doi.org/10.1016/j.jbc.2023.104742
LuÄiÄ, Marina and Wilson, Michael T and Tosha, Takehiko and Sugimoto, Hiroshi and Shilova, Anastasya and Axford, Danny and Owen, Robin L and Hough, Michael A and Worrall, Jonathan AR (2022) Serial Femtosecond Crystallography Reveals the Role of Water in the One- or Two-Electron Redox Chemistry of Compound i in the Catalytic Cycle of the B-Type Dye-Decolorizing Peroxidase DtpB. ACS Catalysis, 12 (21). pp. 13349-13359. DOI https://doi.org/10.1021/acscatal.2c03754
Ukeri, John and Wilson, Michael T and Reeder, Brandon J (2022) Modulating Nitric Oxide Dioxygenase and Nitrite Reductase of Cytoglobin through Point Mutations. Antioxidants, 11 (9). p. 1816. DOI https://doi.org/10.3390/antiox11091816
Wilson, Michael T and Reeder, Brandon J (2022) The peroxidatic activities of Myoglobin and Hemoglobin, their pathological consequences and possible medical interventions. Molecular Aspects of Medicine, 84. p. 101045. DOI https://doi.org/10.1016/j.mam.2021.101045
LuÄiÄ, Marina and Wilson, Michael T and Svistunenko, Dimitri A and Owen, Robin L and Hough, Michael A and Worrall, Jonathan AR (2021) Aspartate or arginine? Validated redox state X-ray structures elucidate mechanistic subtleties of FeIVâ=âO formation in bacterial dye-decolorizing peroxidases. Journal of Biological Inorganic Chemistry, 26 (7). pp. 743-761. DOI https://doi.org/10.1007/s00775-021-01896-2
Svistunenko, Dimitri A and Pullin, Jacob and Bradley, Justin and Moore, Geoffrey and Le Brun, Nick and Wilson, Michael (2021) Electron transfer from haem to the diâiron ferroxidase centre in bacterioferritin. Angewandte Chemie International Edition, 60 (15). pp. 8376-8379. DOI https://doi.org/10.1002/anie.202015965
Pullin, Jacob and Wilson, Michael T and ClĂŠmancey, Martin and Blondin, Geneviève and Bradley, Justin M and Moore, Geoffrey R and Le Brun, Nick E and LuÄiÄ, Marina and Worrall, Jonathan AR and Svistunenko, Dimitri A (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). pp. 8361-8369. DOI https://doi.org/10.1002/anie.202015964
Lucic, Marina and Chaplin, Amanda K and Moreno-Chicano, Tadeo and Dworkowski, Florian and Wilson, Michael and Svistunenko, Dimitri and Hough, Michael and Worrall, Jonathan AR (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). pp. 1620-1636. DOI https://doi.org/10.1039/c9dt04583j
Straw, Megan L and Hough, Michael A and Wilson, Michael T and Worrall, Jonathan AR (2019) A histidine residue and a tetranuclear cuprousâthiolate cluster dominate the copper loading landscape of a copper storage protein from Streptomyces lividans. Chemistry â A European Journal, 25 (45). pp. 10678-10688. DOI https://doi.org/10.1002/chem.201901411
Deacon, Oliver M and Svistunenko, Dimitri A and Moore, Geoffrey R and Wilson, Michael T and Worrall, Jonathan AR (2018) Naturally Occurring Disease-Related Mutations in the 40â57 Ί-Loop of Human Cytochrome c Control Triggering of the Alkaline Isomerization. Biochemistry, 57 (29). pp. 4276-4288. DOI https://doi.org/10.1021/acs.biochem.8b00520
Voong, CP and Spencer, PS and Navarrete, CV and Turner, D and Hayrabedyan, SB and Crummy, P and Holloway, E and Wilson, MT and Smith, PR and FernĂĄndez, 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-. DOI https://doi.org/10.3389/fgene.2017.00182
Chaplin, AK and 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). pp. 9420-9429. DOI https://doi.org/10.1039/c7dt01144j
Chaplin, AK and Svistunenko, DA and Hough, MA and Wilson, MT and 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). pp. 809-825. DOI https://doi.org/10.1042/BCJ20160968
Welbourn, Elizabeth M and Wilson, Michael T and Yusof, Ashril and Metodiev, Metodi V and Cooper, Chris E (2017) The mechanism of formation, structure and physiological relevance of covalent hemoglobin attachment to the erythrocyte membrane. Free Radical Biology and Medicine, 103. pp. 95-106. DOI https://doi.org/10.1016/j.freeradbiomed.2016.12.024
Karsisiotis, AI and Deacon, OM and Wilson, MT and Macdonald, C and Blumenschein, TMA and Moore, GR and Worrall, JAR (2016) Increased dynamics in the 40â57 Ί-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation. Scientific Reports, 6 (1). 30447-. DOI https://doi.org/10.1038/srep30447
Chaplin, Amanda K and Wilson, Michael T and Hough, Michael A and Svistunenko, Dimitri A and Hemsworth, Glyn R and Walton, Paul H and Vijgenboom, Erik and Worrall, Jonathan AR (2016) Heterogeneity in the Histidine-brace Copper Coordination Sphere in Auxiliary Activity Family 10 (AA10) Lytic Polysaccharide Monooxygenases. Journal of Biological Chemistry, 291 (24). pp. 12838-12850. DOI https://doi.org/10.1074/jbc.m116.722447
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.
Ghafoor, Dlzar D and Kekilli, Demet and Abdullah, Gaylany H and Dworkowski, Florian SN and Hassan, Hamid G and Wilson, Michael T and Strange, Richard W and Hough, Michael A (2015) Hydrogen bonding of the dissociated histidine ligand is not required for formation of a proximal NO adduct in cytochrome câ. JBIC Journal of Biological Inorganic Chemistry, 20 (6). pp. 949-956. DOI https://doi.org/10.1007/s00775-015-1278-y
Silaghi-Dumitrescu, Radu and Scurtu, Florina and Mason, Maria G and Svistunenko, Dimitri A and Wilson, Michael T and Cooper, Chris E (2015) The reaction of oxyhemoglobin with nitric oxide: EPR evidence for an iron(III)-nitrate intermediate. Inorganica Chimica Acta, 436. pp. 179-183. DOI https://doi.org/10.1016/j.ica.2015.07.037
Manole, Andreea and Kekilli, Demet and Svistunenko, Dimitri A and Wilson, Michael T and Dobbin, Paul S and Hough, Michael A (2015) Conformational control of the binding of diatomic gases to cytochrome câ˛. JBIC Journal of Biological Inorganic Chemistry, 20 (4). pp. 675-686. DOI https://doi.org/10.1007/s00775-015-1253-7
Beckerson, Penny and Reeder, Brandon J and Wilson, Michael T (2015) Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding. FEBS Letters, 589 (4). pp. 507-512. DOI https://doi.org/10.1016/j.febslet.2015.01.010
Porto, Tatiana V and Wilson, Michael T and Worrall, Jonathan AR (2015) Copper and nickel bind via two distinct kinetic mechanisms to a CsoR metalloregulator. Dalton Transactions, 44 (46). pp. 20176-20185. DOI https://doi.org/10.1039/c5dt03484a
Beckerson, Penny and Wilson, Michael T and Svistunenko, Dimitri A and Reeder, Brandon J (2015) Cytoglobin ligand binding regulated by changing haem-co-ordination in response to intramolecular disulfide bond formation and lipid interaction. Biochemical Journal, 465 (1). pp. 127-137. DOI https://doi.org/10.1042/bj20140827
Ascenzi, P and Coletta, M and Wilson, MT and Fiorucci, L and Marino, M and Polticelli, F and 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). pp. 98-109. DOI https://doi.org/10.1002/iub.1350
van Wilderen, LJGW and Silkstone, G and Mason, MG and 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). pp. 885-892. DOI https://doi.org/10.1016/j.fob.2015.10.007
Kassa, T and Jana, S and Strader, MB and Meng, F and Jia, Y and 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). pp. 27939-27958. DOI https://doi.org/10.1074/jbc.m115.651257
Lobato, L and Bouzhir-Sima, L and Yamashita, T and Wilson, MT and 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). pp. 26514-26524. DOI https://doi.org/10.1074/jbc.m114.571398
Hough, Michael A and Silkstone, Gary and Worrall, JAR and Wilson, Michael T (2014) NO Binding to the Proapoptotic Cytochrome câCardiolipin Complex. NITRIC OXIDE, 96. pp. 193-209. DOI https://doi.org/10.1016/b978-0-12-800254-4.00008-8
Strader, MB and Hicks, WA and Kassa, T and Singleton, E and Soman, J and Olson, JS and Weiss, MJ and Mollan, TL and 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). pp. 22342-22357. DOI https://doi.org/10.1074/jbc.m114.568980
Ashe, D and Alleyne, T and Wilson, MT and 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. pp. 36-43. DOI https://doi.org/10.1016/j.abb.2014.04.015
Nicholls, P and Marshall, DCA and 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.
Rong, Zimei and Alayash, Abdu I and Wilson, Michael T and Cooper, Chris E (2013) Modulating hemoglobin nitrite reductase activity through allostery: A mathematical model. Nitric Oxide, 35. pp. 193-198. DOI https://doi.org/10.1016/j.niox.2013.10.007
Nicholls, Peter and Marshall, Doug C and Cooper, Chris E and Wilson, Mike T (2013) Sulfide inhibition of and metabolism by cytochrome <i>c</i> oxidase. Biochemical Society Transactions, 41 (5). pp. 1312-1316. DOI https://doi.org/10.1042/bst20130070
Ascenzi, Paolo and Marino, Maria and Polticelli, Fabio and Coletta, Massimo and Gioia, Magda and Marini, Stefano and Pesce, Alessandra and Nardini, Marco and Bolognesi, Martino and Reeder, Brandon J and Wilson, Michael T (2013) Non-covalent and covalent modifications modulate the reactivity of monomeric mammalian globins. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1834 (9). pp. 1750-1756. DOI https://doi.org/10.1016/j.bbapap.2013.02.012
Rong, Zimei and Wilson, Michael T and Cooper, Chris E (2013) A model for the nitric oxide producing nitrite reductase activity of hemoglobin as a function of oxygen saturation. Nitric Oxide, 33. pp. 74-80. DOI https://doi.org/10.1016/j.niox.2013.06.008
Cooper, Chris E and Schaer, Dominik J and Buehler, Paul W and Wilson, Michael T and Reeder, Brandon J and Silkstone, Gary and Svistunenko, Dimitri A and Bulow, Leif and Alayash, Abdu I (2013) Haptoglobin Binding Stabilizes Hemoglobin Ferryl Iron and the Globin Radical on Tyrosine β145. Antioxidants & Redox Signaling, 18 (17). pp. 2264-2273. DOI https://doi.org/10.1089/ars.2012.4547.test
Reeder, Brandon J and Svistunenko, Dimitri A and Cooper, Chris E and Wilson, Michael T (2012) Engineering Tyrosine-Based Electron Flow Pathways in Proteins: The Case of Aplysia Myoglobin. Journal of the American Chemical Society, 134 (18). pp. 7741-7749. DOI https://doi.org/10.1021/ja211745g
Rajagopal, Badri S and Silkstone, Gary G and Nicholls, Peter and Wilson, Michael T and Worrall, Jonathan AR (2012) An investigation into a cardiolipin acyl chain insertion site in cytochrome c. Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1817 (5). pp. 780-791. DOI https://doi.org/10.1016/j.bbabio.2012.02.010
Marshall, DCA and Nicholls, P and 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 and 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.
Rajagopal, Badri S and Wilson, Michael T and Bendall, Derek S and Howe, Christopher J and Worrall, Jonathan AR (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). pp. 577-588. DOI https://doi.org/10.1007/s00775-011-0758-y
Reeder, BJ and 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). pp. 483-492. DOI https://doi.org/10.1042/bj20101136
Boutaud, Olivier and Moore, Kevin P and Reeder, Brandon J and Harry, David and Howie, Alexander J and Wang, Shuhe and Carney, Clare K and Masterson, Tina S and Amin, Taneem and Wright, David W and Wilson, Michael T and Oates, John A and Roberts, L Jackson (2010) Acetaminophen inhibits hemoprotein-catalyzed lipid peroxidation and attenuates rhabdomyolysis-induced renal failure. Proceedings of the National Academy of Sciences, 107 (6). pp. 2699-2704. DOI https://doi.org/10.1073/pnas.0910174107
Cooper, CE and Holladay, R and Nicholls, P and Svistunenko, DA and Mason, MG and 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 and Kapetanaki, SM and Husu, I and 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). pp. 19785-92.
Godoy, LC and Munoz-Pinedo, C and Castro, L and Cardaci, S and Schonhoff, CM and King, M and Tortora, V and Marin, M and Miao, Q and Jiang, JF and Kapralov, A and Jemmerson, R and Silkstone, GG and Patel, JN and Evans, JE and Wilson, MT and Green, DR and Kagan, VE and 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). pp. 2653-2658. DOI https://doi.org/10.1073/pnas.0809279106
Kapetanaki, SM and Silkstone, G and Husu, I and Liebl, U and Wilson, MT and Vos, MH (2009) Interaction of Carbon Monoxide with the Apoptosis-Inducing Cytochrome c-Cardiolipin Complex. Biochemistry, 48 (7). pp. 1613-1619. DOI https://doi.org/10.1021/bi801817v
Reeder, Brandon J and Grey, Marie and Silaghi-Dumitrescu, Radu-Lucian and Svistunenko, Dimitri A and BĂźlow, Leif and Cooper, Chris E and Wilson, Michael T (2008) Tyrosine Residues as Redox Cofactors in Human Hemoglobin. Journal of Biological Chemistry, 283 (45). pp. 30780-30787. DOI https://doi.org/10.1074/jbc.m804709200
Reeder, Brandon J and Hider, Robert C and Wilson, Michael T (2008) Iron chelators can protect against oxidative stress through ferryl heme reduction. Free Radical Biology and Medicine, 44 (3). pp. 264-273. DOI https://doi.org/10.1016/j.freeradbiomed.2007.08.006
Reeder, Brandon J and Cutruzzola, Francesca and Bigotti, Maria Giulia and Hider, Robert C and Wilson, Michael T (2008) Tyrosine as a redox-active center in electron transfer to ferryl heme in globins. Free Radical Biology and Medicine, 44 (3). pp. 274-283. DOI https://doi.org/10.1016/j.freeradbiomed.2007.06.030
Wilson, Michael T and Reeder, Brandon J (2008) Oxygenâbinding haem proteins. Experimental Physiology, 93 (1). pp. 128-132. DOI https://doi.org/10.1113/expphysiol.2007.039735
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). pp. 1103-1105. DOI https://doi.org/10.1042/bst0361103