Professor Jonathan Worrall

Moreno-Chicano, T., Carey, LM., Axford, D., Beale, JH., Doak, RB., Duyvesteyn, HME., Ebrahim, A., Henning, RW., Monteiro, DCF., Myles, DA., Owada, S., Sherrell, DA., Straw, ML., Šrajer, V., Sugimoto, H., Tono, K., Tosha, T., Tews, I., Trebbin, M., Strange, RW., Weiss, KL., Worrall, JAR., Meilleur, F., Owen, RL., Ghiladi, RA. and Hough, MA., (2022). Complementarity of neutron, XFEL and synchrotron crystallography for defining the structures of metalloenzymes at room temperature. IUCrJ. 9 (5), 610-624

Worrall, JAR. and Hough, MA., (2022). Serial femtosecond crystallography approaches to understanding catalysis in iron enzymes.. Current Opinion in Structural Biology. 77, 102486-102486

Lučić, M., Wilson, MT., Tosha, T., Sugimoto, H., Shilova, A., Axford, D., Owen, RL., Hough, MA. and Worrall, JAR., (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), 13349-13359

Munir, A., Wilson, MT., Hardwick, SW., Chirgadze, DY., Worrall, JAR., Blundell, TL. and Chaplin, AK., (2021). Using cryo-EM to understand antimycobacterial resistance in the catalase-peroxidase (KatG) from Mycobacterium tuberculosis. Structure. 29 (8), 899-912.e4

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

Horrell, S., Axford, D., Devenish, NE., Ebrahim, A., Hough, MA., Sherrell, DA., Storm, SLS., Tews, I., Worrall, JAR. and Owen, RL., (2021). Fixed Target Serial Data Collection at Diamond Light Source.. Journal of Visualized Experiments. 2021 (168)

Deacon, OM., White, RW., Moore, GR., Wilson, MT. and Worrall, JAR., (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, 110924-110924

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

Lucic, M., Svistunenko, D., Wilson, M., Chaplin, A., Davy, B., Ebrahim, A., Axford, D., Tosha, T., Sugimoto, H., Owada, S., Dworkowski, F., Tews, I., Owen, R., Hough, M. and Worrall, JAR., (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), 21656-21662

Lučić, M., Svistunenko, DA., Wilson, MT., Chaplin, AK., Davy, B., Ebrahim, A., Axford, D., Tosha, T., Sugimoto, H., Owada, S., Dworkowski, FSN., Tews, I., Owen, RL., Hough, MA. and Worrall, JAR., (2020). Serial Femtosecond Zero Dose Crystallography Captures a Water‐Free Distal Heme Site in a Dye‐Decolorising Peroxidase to Reveal a Catalytic Role for an Arginine in Fe^IV=O Formation. Angewandte Chemie. 132 (48), 21840-21846

Chaplin, AK., Chicano, TM., Hampshire, BV., Wilson, MT., Hough, MA., Svistunenko, DA. and Worrall, JAR., (2019). An Aromatic Dyad Motif in Dye Decolourising Peroxidases Has Implications for Free Radical Formation and Catalysis. Chemistry – A European Journal. 25 (24), 6141-6153

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

Ebrahim, A., Moreno-Chicano, T., Appleby, MV., Chaplin, AK., Beale, JH., Sherrell, DA., Duyvesteyn, HME., Owada, S., Tono, K., Sugimoto, H., Strange, RW., Worrall, JAR., Axford, D., Owen, RL. and Hough, MA., (2019). Dose-resolved serial synchrotron and XFEL structures of radiation-sensitive metalloproteins. IUCrJ. 6 (4), 543-551

Moreno-Chicano, T., Ebrahim, A., Axford, D., Appleby, MV., Beale, JH., Chaplin, AK., Duyvesteyn, HME., Ghiladi, RA., Owada, S., Sherrell, DA., Strange, RW., Sugimoto, H., Tono, K., Worrall, JAR., Owen, RL. and Hough, MA., (2019). High-throughput structures of protein–ligand complexes at room temperature using serial femtosecond crystallography. IUCrJ. 6 (6), 1074-1085

Beale, JH., Bolton, R., Marshall, SA., Beale, EV., Carr, SB., Ebrahim, A., Moreno-Chicano, T., Hough, MA., Worrall, JAR., Tews, I. and Owen, RL., (2019). Successful sample preparation for serial crystallography experiments. Journal of Applied Crystallography. 52 (6), 1385-1396

Straw, ML., Chaplin, AK., Hough, MA., Paps, J., Bavro, VN., Wilson, MT., Vijgenboom, E. and Worrall, JAR., (2018). A cytosolic copper storage protein provides a second level of copper tolerance in Streptomyces lividans.. Metallomics: integrated biometal science. 2018 (10), 180-193

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

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

Karsisiotis, AI., Deacon, OM., Macdonald, C., Blumenschein, TMA., Moore, GR. and Worrall, JAR., (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), 165-168

Chaplin, AK., Bernini, C., Sinicropi, A., Basosi, R., Worrall, JAR. and Svistunenko, DA., (2017). Tyrosine or Tryptophan? Modifying a Metalloradical Catalytic Site by Removal of the Cys–Tyr Cross‐Link in the Galactose 6‐Oxidase Homologue GlxA. Angewandte Chemie International Edition. 129 (23), 6602-6606

Kekilli, D., Moreno-Chicano, T., Chaplin, AK., Horrell, S., Dworkowski, FSN., Worrall, JAR., Strange, RW. and Hough, MA., (2017). Photoreduction and validation of haem?ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction. IUCrJ. 4 (3), 263-270

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

Deacon, OM., Karsisiotis, AI., Moreno-Chicano, T., Hough, MA., Macdonald, C., Blumenschein, TMA., Wilson, MT., Moore, GR. and Worrall, JAR., (2017). Heightened Dynamics of the Oxidized Y48H Variant of Human Cytochrome c Increases Its Peroxidatic Activity.. Biochemistry. 56 (46), 6111-6124

Chaplin, AK., Bernini, C., Sinicropi, A., Basosi, R., Worrall, JAR. and Svistunenko, DA., (2017). Tyrosine or Tryptophan? Modifying a Metalloradical Catalytic Site by Removal of the Cys–Tyr Cross‐Link in the Galactose 6‐Oxidase Homologue GlxA. Angewandte Chemie. 129 (23), 6602-6606

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

Petrus, MLC., Vijgenboom, E., Chaplin, AK., Worrall, JAR., van Wezel, GP. and Claessen, D., (2016). The DyP-type peroxidase DtpA is a Tat-substrate required for GlxA maturation and morphogenesis in Streptomyces. Open Biology. 6 (1), 150149-150149

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-

Chaplin, AK., Tan, BG., Vijgenboom, E. and Worrall, JAR., (2015). Copper trafficking in the CsoR regulon of Streptomyces lividans. Metallomics. 7 (1), 145-155

Chaplin, AK., Petrus, MLC., Mangiameli, G., Hough, MA., Svistunenko, DA., Nicholls, P., Claessen, D., Vijgenboom, E. and Worrall, JAR., (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 Streptomyces lividans. Biochemical Journal. 469 (3), 433-444

Porto, TV., Hough, MA. and Worrall, JAR., (2015). Structural insights into conformational switching in the copper metalloregulator CsoR fromStreptomyces lividans. Acta Crystallographica Section D Biological Crystallography. 71 (9), 1872-1878

Karsisiotis, AI., Deacon, OM., Rajagopal, BS., Macdonald, C., Blumenschein, TMA., Moore, GR. and Worrall, JAR., (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), 415-419

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

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

Blundell, KLIM., Hough, MA., Vijgenboom, E. and Worrall, JAR., (2014). Structural and mechanistic insights into an extracytoplasmic copper trafficking pathway in Streptomyces lividans. Biochemical Journal. 459 (3), 525-538

Tan, BG., Vijgenboom, E. and Worrall, JAR., (2014). Conformational and thermodynamic hallmarks of DNA operator site specificity in the copper sensitive operon repressor from Streptomyces lividans. Nucleic Acids Research. 42 (2), 1326-1340

Rajagopal, BS., Edzuma, AN., Hough, MA., Blundell, KLIM., Kagan, VE., Kapralov, AA., Fraser, LA., Butt, JN., Silkstone, GG., Wilson, MT., Svistunenko, DA. and Worrall, JAR., (2013). The hydrogen-peroxide-induced radical behaviour in human cytochrome c–phospholipid complexes: implications for the enhanced pro-apoptotic activity of the G41S mutant. Biochemical Journal. 456 (3), 441-452

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), 120163-120163

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), 10608-10608

Dwarakanath, S., Chaplin, AK., Hough, MA., Rigali, S., Vijgenboom, E. and Worrall, JAR., (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), 17833-17847

Svistunenko, DA., Worrall, JAR., Chugh, SB., Haigh, SC., Ghiladi, RA. and Nicholls, P., (2012). Ferric haem forms of Mycobacterium tuberculosis catalase-peroxidase probed by EPR spectroscopy: Their stability and interplay with pH. Biochimie. 94 (6), 1274-1280

Mason, JM., Bendall, DS., Howe, CJ. and Worrall, JAR., (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), 311-318

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

Bischin, C., Deac, F., Silaghi-Dumitrescu, R., Worrall, JAR., Rajagopal, BS., Damian, G. and Cooper, CE., (2011). Ascorbate peroxidase activity of cytochromec. Free Radical Research. 45 (4), 439-444

Worrall, JAR. and Mason, JM., (2011). Thermodynamic analysis of Jun-Fos coiled coil peptide antagonists. FEBS Journal. 278 (4), 663-672

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

Volkov, AN., Nicholls, P. and Worrall, JAR., (2011). The complex of cytochrome c and cytochrome c peroxidase: The end of the road?. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1807 (11), 1482-1503

Worrall, JAR. and Vijgenboom, E., (2010). Copper mining in Streptomyces: enzymes, natural products and development. Natural Product Reports. 27 (5), 742-742

Volkov, AN., Bashir, Q., Worrall, JAR., Ullmann, GM. and Ubbink, M., (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), 11487-11495

Volkov, AN., Bashir, Q., Worrall, JAR. and Ubbink, M., (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), 1003-1013

Worrall, JAR., Górna, M., Crump, NT., Phillips, LG., Tuck, AC., Price, AJ., Bavro, VN. and Luisi, BF., (2008). Reconstitution and analysis of the multienzyme Escherichia coli RNA degradosome.. Journal of Molecular Biology. 382 (4), 870-883

Worrall, JAR., Howe, FS., McKay, AR., Robinson, CV. and Luisi, BF., (2008). Allosteric Activation of the ATPase Activity of the Escherichia coli RhlB RNA Helicase. Journal of Biological Chemistry. 283 (9), 5567-5576

Worrall, JAR., Luisi, BF., Schlarb-Ridley, BG., Bendall, DS. and Howe, CJ., (2008). Cytochrome c6A: discovery, structure and properties responsible for its low haem redox potential. Biochemical Society Transactions. 36 (6), 1175-1179

Worrall, JAR. and Luisi, BF., (2007). Information available at cut rates: structure and mechanism of ribonucleases. Current Opinion in Structural Biology. 17 (1), 128-137

Worrall, JAR., Górna, M., Pei, XY., Spring, DR., Nicholson, RL. and Luisi, BF., (2007). Design and chance in the self-assembly of macromolecules. Biochemical Society Transactions. 35 (3), 502-507

Worrall, JAR., Schlarb-Ridley, BG., Reda, T., Marcaida, MJ., Moorlen, RJ., Wastl, J., Hirst, J., Bendall, DS., Luisi, BF. and Howe, CJ., (2007). Modulation of Heme Redox Potential in the Cytochrome c₆ Family. Journal of the American Chemical Society. 129 (30), 9468-9475

Volkov, AN., Worrall, JAR., Holtzmann, E. and Ubbink, M., (2006). Solution structure and dynamics of the complex between cytochromecand cytochromecperoxidase determined by paramagnetic NMR. Proceedings of the National Academy of Sciences. 103 (50), 18945-18950

Marcaida, MJ., Schlarb-Ridley, BG., Worrall, JAR., Wastl, J., Evans, TJ., Bendall, DS., Luisi, BF. and Howe, CJ., (2006). Structure of Cytochrome c6A, a Novel Dithio-cytochrome of Arabidopsis thaliana, and its Reactivity with Plastocyanin: Implications for Function. Journal of Molecular Biology. 360 (5), 968-977

Worrall, JAR., Machczynski, MC., Keijser, BJF., di Rocco, G., Ceola, S., Ubbink, M., Vijgenboom, E. and Canters, GW., (2006). Spectroscopic Characterization of a High-Potential Lipo-Cupredoxin Found in Streptomyces coelicolor. Journal of the American Chemical Society. 128 (45), 14579-14589

(2006). CORRECTION. Protein Science. 15 (6), 1563-1563

Volkov, AN., Ferrari, D., Worrall, JAR., Bonvin, AMJJ. and Ubbink, M., (2006). The orientations of cytochrome c in the highly dynamic complex with cytochrome b(5) visualized by NMR and docking using HADDOCK (vol 14, pg 799, 2005). PROTEIN SCIENCE. 15 (6), 1563-1563

Worrall, JAR., van Roon, AM., Ubbink, M. and Canters, GW., (2005). The effect of replacing the axial methionine ligand with a lysine residue in cytochrome c‐550 from Paracoccus versutus assessed by X‐ray crystallography and unfolding. The FEBS Journal. 272 (10), 2441-2455

Volkov, AN., Ferrari, D., Worrall, JAR., Bonvin, AMJJ. and Ubbink, M., (2005). The orientations of cytochrome c in the highly dynamic complex with cytochrome b₅ visualized by NMR and docking using HADDOCK. Protein Science. 14 (3), 799-811

Worrall, JAR., Diederix, REM., Prudêncio, M., Lowe, CE., Ciofi‐Baffoni, S., Ubbink, M. and Canters, GW., (2005). The Effects of Ligand Exchange and Mobility on the Peroxidase Activity of a Bacterial Cytochrome c upon Unfolding. ChemBioChem. 6 (4), 747-758

Diederix, REM., Fittipaldi, M., Worrall, JAR., Huber, M., Ubbink, M. and Canters, GW., (2003). Kinetic Stability of the Peroxidase Activity of Unfolded Cytochrome c:  Heme Degradation and Catalyst Inactivation by Hydrogen Peroxide. Inorganic Chemistry. 42 (22), 7249-7257

Worrall, JAR., Reinle, W., Bernhardt, R. and Ubbink, M., (2003). Transient Protein Interactions Studied by NMR Spectroscopy:  The Case of Cytochrome c and Adrenodoxin. Biochemistry. 42 (23), 7068-7076

Crowley, PB., Rabe, KS., Worrall, JAR., Canters, GW. and Ubbink, M., (2002). The Ternary Complex of Cytochrome f and Cytochrome c: Identification of a Second Binding Site and Competition for Plastocyanin Binding. ChemBioChem. 3 (6), 526-526

Ubbink, M., Worrall, JAR., Canters, GW., Groenen, EJJ. and Huber, M., (2002). Paramagnetic Resonance of Biological Metal Centers. Annual Review of Biophysics and Biomolecular Structure. 31 (1), 393-422

Worrall, JAR., Liu, Y., Crowley, PB., Nocek, JM., Hoffman, BM. and Ubbink, M., (2002). Myoglobin and Cytochrome b₅:  A Nuclear Magnetic Resonance Study of a Highly Dynamic Protein Complex. Biochemistry. 41 (39), 11721-11730

Crowley, PB., Rabe, KS., Worrall, JAR., Canters, GW. and Ubbink, M., (2002). The ternary complex of cytochrome f and cytochrome c: Identification of a second binding site and competition for plastocyanin binding. ChemBioChem. 3 (6), 526-533

Worrall, JAR., Kolczak, U., Canters, GW. and Ubbink, M., (2001). Interaction of Yeast Iso-1-cytochrome c with Cytochrome c Peroxidase Investigated by [¹⁵N,¹H] Heteronuclear NMR Spectroscopy. Biochemistry. 40 (24), 7069-7076

Im, S-C., Worrall, JAR., Liu, G., Aliverti, A., Zanetti, G., Luchinat, C., Bertini, I. and Sykes, AG., (2000). The Cr^IIL Reduction of [2Fe-2S] Ferredoxins and Site of Attachment of Cr^III Using ¹H NMR and Site-Directed Mutagenesis. Inorganic Chemistry. 39 (8), 1755-1764