Items where Author is "Worrall, Jonathan AR"

Bolton, Rachel and Machelett, Moritz M and Worrall, Jonathan AR and Hough, Michael A and et al. (2024) A redox switch allows binding of Fe(II) and Fe(III) ions in the cyanobacterial iron-binding protein FutA from Prochlorococcus. Proceedings of the National Academy of Sciences of the United States of America, 121 (12). e2308478121-. DOI https://doi.org/10.1073/pnas.2308478121

Worrall, Jonathan AR and Hough, Michael A (2022) Serial femtosecond crystallography approaches to understanding catalysis in iron enzymes. Current Opinion in Structural Biology, 77. p. 102486. DOI https://doi.org/10.1016/j.sbi.2022.102486

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

Moreno-Chicano, Tadeo and Carey, Leiah M and Axford, Danny and Beale, John H and Doak, R Bruce and Duyvesteyn, Helen ME and Ebrahim, Ali and Henning, Robert W and Monteiro, Diana CF and Myles, Dean A and Owada, Shigeki and Sherrell, Darren A and Straw, Megan L and Šrajer, Vukica and Sugimoto, Hiroshi and Tono, Kensuke and Tosha, Takehiko and Tews, Ivo and Trebbin, Martin and Strange, Richard W and Weiss, Kevin L and Worrall, Jonathan AR and Meilleur, Flora and Owen, Robin L and Ghiladi, Reza A and Hough, Michael A (2022) Complementarity of neutron, XFEL and synchrotron crystallography for defining the structures of metalloenzymes at room temperature. IUCrJ, 9 (5). pp. 610-624. DOI https://doi.org/10.1107/s2052252522006418

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

Worrall, Jonathan AR (2021) Copper Storage Protein From Streptomyces Lividans. In: Encyclopedia of Inorganic and Bioinorganic Chemistry (EIBC). Wiley, pp. 1-16. ISBN 9781119951438. Official URL: https://doi.org/10.1002/9781119951438.eibc2777

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

Horrell, Sam and Axford, Danny and Devenish, Nicholas E and Ebrahim, Ali and Hough, Michael A and Sherrell, Darren A and Storm, Selina LS and Tews, Ivo and Worrall, Jonathan AR and Owen, Robin L (2021) Fixed Target Serial Data Collection at Diamond Light Source. Journal of Visualized Experiments, 2021 (168). DOI https://doi.org/10.3791/62200

Lucic, Marina and Svistunenko, Dimitri and Wilson, Michael and Chaplin, Amanda and Davy, Bradley and Ebrahim, Ali and Axford, Danny and Tosha, Takehiko and Sugimoto, Hiroshi and Owada, Shigeki and Dworkowski, Florian and Tews, Ivo and Owen, Robin and Hough, Michael and Worrall, Jonathan AR (2020) Serial femtosecond zero dose crystallography captures a water‐free distal heme site in a dye‐decolourising peroxidase to reveal a catalytic role for an arginine in FeIV=O formation. Angewandte Chemie International Edition, 59 (48). pp. 21656-21662. DOI https://doi.org/10.1002/anie.202008622

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

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

Beale, John H and Bolton, Rachel and Marshall, Stephen A and Beale, Emma V and Carr, Stephen B and Ebrahim, Ali and Moreno-Chicano, Tadeo and Hough, Michael A and Worrall, Jonathan AR and Tews, Ivo and Owen, Robin L (2019) Successful sample preparation for serial crystallography experiments. Journal of Applied Crystallography, 52 (6). pp. 1385-1396. DOI https://doi.org/10.1107/s1600576719013517

Moreno-Chicano, Tadeo and Ebrahim, Ali and Axford, Danny and Appleby, Martin V and Beale, John H and Chaplin, Amanda K and Duyvesteyn, Helen ME and Ghiladi, Reza A and Owada, Shigeki and Sherrell, Darren A and Strange, Richard W and Sugimoto, Hiroshi and Tono, Kensuke and Worrall, Jonathan AR and Owen, Robin L and Hough, Michael A (2019) High-throughput structures of protein–ligand complexes at room temperature using serial femtosecond crystallography. IUCrJ, 6 (6). pp. 1074-1085. DOI https://doi.org/10.1107/s2052252519011655

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

Ebrahim, Ali and Moreno-Chicano, Tadeo and Appleby, Martin V and Chaplin, Amanda K and Beale, John H and Sherrell, Darren A and Duyvesteyn, Helen ME and Owada, Shigeki and Tono, Kensuke and Sugimoto, Hiroshi and Strange, Richard W and Worrall, Jonathan AR and Axford, Danny and Owen, Robin L and Hough, Michael A (2019) Dose-resolved serial synchrotron and XFEL structures of radiation-sensitive metalloproteins. IUCrJ, 6 (4). pp. 543-551. DOI https://doi.org/10.1107/s2052252519003956

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

Karsisiotis, Andreas Ioannis and Deacon, Oliver M and Macdonald, Colin and Blumenschein, Tharin MA and Moore, Geoffrey R and Worrall, Jonathan AR (2017) Near-complete backbone resonance assignments of acid-denatured human cytochrome c in dimethylsulfoxide: a prelude to studying interactions with phospholipids. Biomolecular NMR Assignments, 11 (2). pp. 165-168. DOI https://doi.org/10.1007/s12104-017-9740-0

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

Petrus, Marloes LC and Vijgenboom, Erik and Chaplin, Amanda K and Worrall, Jonathan AR and van Wezel, Gilles P and Claessen, Dennis (2016) The DyP-type peroxidase DtpA is a Tat-substrate required for GlxA maturation and morphogenesis in <i>Streptomyces</i>. Open Biology, 6 (1). p. 150149. DOI https://doi.org/10.1098/rsob.150149

Karsisiotis, Andreas Ioannis and Deacon, Oliver M and Rajagopal, Badri S and Macdonald, Colin and Blumenschein, Tharin MA and Moore, Geoffrey R and Worrall, Jonathan AR (2015) Backbone resonance assignments of ferric human cytochrome c and the pro-apoptotic G41S mutant in the ferric and ferrous states. Biomolecular NMR Assignments, 9 (2). pp. 415-419. DOI https://doi.org/10.1007/s12104-015-9621-3

Porto, Tatiana V and Hough, Michael A and Worrall, Jonathan AR (2015) Structural insights into conformational switching in the copper metalloregulator CsoR from<i>Streptomyces lividans</i>. Acta Crystallographica Section D Biological Crystallography, 71 (9). pp. 1872-1878. DOI https://doi.org/10.1107/s1399004715013012

Chaplin, Amanda K and Petrus, Marloes LC and Mangiameli, Giulia and Hough, Michael A and Svistunenko, Dimitri A and Nicholls, Peter and Claessen, Dennis and Vijgenboom, Erik and Worrall, Jonathan AR (2015) GlxA is a new structural member of the radical copper oxidase family and is required for glycan deposition at hyphal tips and morphogenesis of <i>Streptomyces lividans</i>. Biochemical Journal, 469 (3). pp. 433-444. DOI https://doi.org/10.1042/bj20150190

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

Chaplin, Amanda K and Tan, Benedict G and Vijgenboom, Erik and Worrall, Jonathan AR (2015) Copper trafficking in the CsoR regulon of Streptomyces lividans. Metallomics, 7 (1). pp. 145-155. DOI https://doi.org/10.1039/c4mt00250d

Blundell, Katie LIM and Hough, Michael A and Vijgenboom, Erik and Worrall, Jonathan AR (2014) Structural and mechanistic insights into an extracytoplasmic copper trafficking pathway in <i>Streptomyces lividans</i>. Biochemical Journal, 459 (3). pp. 525-538. DOI https://doi.org/10.1042/bj20140017

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

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

Dwarakanath, Srivatsa and Chaplin, Amanda K and Hough, Michael A and Rigali, Sébastien and Vijgenboom, Erik and Worrall, Jonathan AR (2012) Response to Copper Stress in Streptomyces lividans Extends beyond Genes under Direct Control of a Copper-sensitive Operon Repressor Protein (CsoR). Journal of Biological Chemistry, 287 (21). pp. 17833-17847. DOI https://doi.org/10.1074/jbc.m112.352740

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

Mason, Jody M and Bendall, Derek S and Howe, Christopher J and Worrall, Jonathan AR (2012) The role of a disulfide bridge in the stability and folding kinetics of Arabidopsis thaliana cytochrome c6A. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1824 (2). pp. 311-318. DOI https://doi.org/10.1016/j.bbapap.2011.10.015

Bischin, Cristina and Deac, Florina and Silaghi-Dumitrescu, Radu and Worrall, Jonathan AR and Rajagopal, Badri S and Damian, Grigore and Cooper, Chris E (2011) Ascorbate peroxidase activity of cytochrome<i>c</i>. Free Radical Research, 45 (4). pp. 439-444. DOI https://doi.org/10.3109/10715762.2010.540575

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

Worrall, Jonathan AR and Mason, Jody M (2011) Thermodynamic analysis of Jun-Fos coiled coil peptide antagonists. FEBS Journal, 278 (4). pp. 663-672. DOI https://doi.org/10.1111/j.1742-4658.2010.07988.x

Volkov, Alexander N and Bashir, Qamar and Worrall, Jonathan AR and Ullmann, G Matthias and Ubbink, Marcellus (2010) Shifting the Equilibrium between the Encounter State and the Specific Form of a Protein Complex by Interfacial Point Mutations. Journal of the American Chemical Society, 132 (33). pp. 11487-11495. DOI https://doi.org/10.1021/ja100867c

Worrall, Jonathan AR and Vijgenboom, Erik (2010) Copper mining in Streptomyces: enzymes, natural products and development. Natural Product Reports, 27 (5). p. 742. DOI https://doi.org/10.1039/b804465c

Volkov, Alexander N and Bashir, Qamar and Worrall, Jonathan AR and Ubbink, Marcellus (2009) Binding Hot Spot in the Weak Protein Complex of Physiological Redox Partners Yeast Cytochrome c and Cytochrome c Peroxidase. Journal of Molecular Biology, 385 (3). pp. 1003-1013. DOI https://doi.org/10.1016/j.jmb.2008.10.091

Worrall, Jonathan AR and Luisi, Ben F and Schlarb-Ridley, Beatrix G and Bendall, Derek S and Howe, Christopher J (2008) Cytochrome <i>c</i>6A: discovery, structure and properties responsible for its low haem redox potential. Biochemical Society Transactions, 36 (6). pp. 1175-1179. DOI https://doi.org/10.1042/bst0361175

Worrall, Jonathan AR and Górna, Maria and Crump, Nicholas T and Phillips, Lara G and Tuck, Alex C and Price, Amanda J and Bavro, Vassiliy N and Luisi, Ben F (2008) Reconstitution and analysis of the multienzyme Escherichia coli RNA degradosome. Journal of Molecular Biology, 382 (4). pp. 870-883. DOI https://doi.org/10.1016/j.jmb.2008.07.059

Worrall, Jonathan AR and Howe, Françoise S and McKay, Adam R and Robinson, Carol V and Luisi, Ben F (2008) Allosteric Activation of the ATPase Activity of the Escherichia coli RhlB RNA Helicase. Journal of Biological Chemistry, 283 (9). pp. 5567-5576. DOI https://doi.org/10.1074/jbc.m708620200