Items where Author is "Wilson, Michael T"

Lučić, 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

Villar, Irene and Rubio, Maria C and Calvo-Begueria, Laura and Pérez-Rontomé, Carmen and Larrainzar, Estibaliz and Wilson, Michael T and Sandal, Niels and Mur, Luis A and Wang, Longlong and Reeder, Brandon and Duanmu, Deqiang and Uchiumi, Toshiki and Stougaard, Jens and Becana, Manuel (2021) Three classes of hemoglobins are required for optimal vegetative and reproductive growth of Lotus japonicus: genetic and biochemical characterization of LjGlb2-1. Journal of Experimental Botany, 72 (22). pp. 7778-7791. DOI https://doi.org/10.1093/jxb/erab376

Lučić, 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 FeIV = O 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

Munir, Asma and Wilson, Michael T and Hardwick, Steven W and Chirgadze, Dimitri Y and Worrall, Jonathan AR and Blundell, Tom L and Chaplin, Amanda K (2021) Using cryo-EM to understand antimycobacterial resistance in the catalase-peroxidase (KatG) from Mycobacterium tuberculosis. Structure, 29 (8). 899-912.e4. DOI https://doi.org/10.1016/j.str.2020.12.008

Pullin, Jacob and Wilson, Michael T and Clémancey, Martin and Blondin, Geneviève and Bradley, Justin M and Moore, Geoffrey R and Le Brun, Nick E and Lučić, 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

Bradley, Justin M and Svistunenko, Dimitry A and Wilson, Michael T and Hemmings, Andrew M and Moore, Geoffrey R and Le Brun, Nick E (2020) Bacterial iron detoxification at the molecular level. The Journal of Biological Chemistry, 295 (51). pp. 17602-17623. DOI https://doi.org/10.1074/jbc.rev120.007746

Deacon, Oliver M and White, Richard W and Moore, Geoffrey R and Wilson, Michael T and Worrall, Jonathan AR (2020) Comparison of the structural dynamic and mitochondrial electron-transfer properties of the proapoptotic human cytochrome c variants, G41S, Y48H and A51V. Journal of Inorganic Biochemistry, 203. p. 110924. DOI https://doi.org/10.1016/j.jinorgbio.2019.110924

Straw, Megan L and Hough, Michael A and Wilson, Michael T and Worrall, Jonathan AR (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). pp. 10678-10688. DOI https://doi.org/10.1002/chem.201901411

Leiva Eriksson, Nélida and Reeder, Brandon J and Wilson, Michael T and Bülow, Leif (2019) Sugar beet hemoglobins: reactions with nitric oxide and nitrite reveal differential roles for nitrogen metabolism. Biochemical Journal, 476 (14). pp. 2111-2125. DOI https://doi.org/10.1042/bcj20190154

Chaplin, Amanda K and Chicano, Tadeo Moreno and Hampshire, Bethany V and Wilson, Michael T and Hough, Michael A and Svistunenko, Dimitri A and Worrall, Jonathan AR (2019) An Aromatic Dyad Motif in Dye Decolourising Peroxidases Has Implications for Free Radical Formation and Catalysis. Chemistry – A European Journal, 25 (24). pp. 6141-6153. DOI https://doi.org/10.1002/chem.201806290

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 40–57 Ω-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

Straw, Megan L and Chaplin, Amanda K and Hough, Michael A and Paps, Jordi and Bavro, Vassiliy N and Wilson, Michael T and Vijgenboom, Erik and Worrall, Jonathan AR (2018) A cytosolic copper storage protein provides a second level of copper tolerance in Streptomyces lividans. Metallomics: integrated biometal science, 2018 (10). pp. 180-193. DOI https://doi.org/10.1039/c7mt00299h

Kekilli, Demet and Petersen, Christine A and Pixton, David A and Ghafoor, Dlzar D and Abdullah, Gaylany H and Dworkowski, Florian SN and Wilson, Michael T and Heyes, Derren J and Hardman, Samantha JO and Murphy, Loretta M and Strange, Richard W and Scrutton, Nigel S and Andrew, Colin R and Hough, Michael A (2017) Engineering proximal vs. distal heme–NO coordination via dinitrosyl dynamics: implications for NO sensor design. Chemical Science, 8 (3). pp. 1986-1994. DOI https://doi.org/10.1039/c6sc04190f

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

Silkstone, Gary GA and Silkstone, Rebecca S and Wilson, Michael T and Simons, Michelle and Bülow, Leif and Kallberg, Kristian and Ratanasopa, Khuanpiroon and Ronda, Luca and Mozzarelli, Andrea and Reeder, Brandon J and Cooper, Chris E (2016) Engineering tyrosine electron transfer pathways decreases oxidative toxicity in hemoglobin: implications for blood substitute design. Biochemical Journal, 473 (19). pp. 3371-3383. DOI https://doi.org/10.1042/bcj20160243

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

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 c’. 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 c′. 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

Hough, Michael A and Silkstone, Gary and Worrall, JAR and Wilson, Michael T (2014) NO Binding to the Proapoptotic Cytochrome c–Cardiolipin Complex. NITRIC OXIDE, 96. pp. 193-209. DOI https://doi.org/10.1016/b978-0-12-800254-4.00008-8

Rajagopal, Badri S and Edzuma, Ann N and Hough, Michael A and Blundell, Katie LIM and Kagan, Valerian E and Kapralov, Alexandr A and Fraser, Lewis A and Butt, Julea N and Silkstone, Gary G and Wilson, Michael T and Svistunenko, Dimitri A and Worrall, Jonathan AR (2013) The hydrogen-peroxide-induced radical behaviour in human cytochrome <i>c</i>–phospholipid complexes: implications for the enhanced pro-apoptotic activity of the G41S mutant. Biochemical Journal, 456 (3). pp. 441-452. DOI https://doi.org/10.1042/bj20130758

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

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 &amp; Redox Signaling, 18 (17). pp. 2264-2273. DOI https://doi.org/10.1089/ars.2012.4547.test

Blundell, Katie LIM and Wilson, Michael T and Svistunenko, Dimitri A and Vijgenboom, Erik and Worrall, Jonathan AR (2013) Morphological development and cytochrome <i>c</i> oxidase activity in <i>Streptomyces lividans</i> are dependent on the action of a copper bound Sco protein. Open Biology, 3 (1). p. 120163. DOI https://doi.org/10.1098/rsob.120163

Blundell, Katie LIM and Wilson, Michael T and Vijgenboom, Erik and Worrall, Jonathan AR (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). p. 10608. DOI https://doi.org/10.1039/c3dt50540e

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

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

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

Reeder, Brandon J and Svistunenko, Dimitri A and Cooper, Chris E and Wilson, Michael T (2009) Engineering Electron Transfer Pathways in Myoglobin and Hemoglobin: A Route to Detoxify Blood Substitutes? In: UNSPECIFIED, ? - ?.

Reeder, Brandon J and Grey, Marie and Silaghi-Dumitrescu, Radu-Lucian and Svistunenko, Dimitri A and Bülow, 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) Oxygen‐binding haem proteins. Experimental Physiology, 93 (1). pp. 128-132. DOI https://doi.org/10.1113/expphysiol.2007.039735