Dr Dimitri Svistunenko

Nash, BW., Fernandes, TM., Burton, JAJ., Morgado, L., van Wonderen, JH., Svistunenko, DA., Edwards, MJ., Salgueiro, CA., Butt, JN. and Clarke, TA., (2024). Tethered heme domains in a triheme cytochrome allow for increased electron transport distances. Protein Science. 33 (11), e5200-

Adams, HR., Svistunenko, DA., Wilson, MT., Fujii, S., Strange, RW., Hardy, ZA., Vazquez, PA., Dabritz, T., Streblow, GJ., Andrew, CR. and Hough, MA., (2023). A heme pocket aromatic quadrupole modulates gas binding to cytochrome c'-β: Implications for NO sensors.. Journal of Biological Chemistry. 299 (6), 104742-104742

Lučić, M., Wilson, MT., Pullin, J., Hough, MA., Svistunenko, DA. and Worrall, JAR., (2023). New insights into controlling radical migration pathways in heme enzymes gained from the study of a dye-decolorising peroxidase. Chemical Science. 14 (44), 12518-12534

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

Hindson, SA., Bunzel, HA., Frank, B., Svistunenko, DA., Williams, C., van der Kamp, MW., Mulholland, AJ., Pudney, CR. and Anderson, JLR., (2021). Rigidifying a De Novo Enzyme Increases Activity and Induces a Negative Activation Heat Capacity.. ACS Catalysis. 11 (18), 11532-11541

Svistunenko, DA., (2021). EPR spectroscopy of whole blood and blood components: can we diagnose abnormalities?. Journal of biomedical research. 35 (4), 294-300

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

Svistunenko, DA. and Manole, A., (2020). Tyrosyl radical in haemoglobin and haptoglobin-haemoglobin complex: how does haptoglobin make haemoglobin less toxic?. The Journal of Biomedical Research. 34 (4), 281-281

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

Bradley, JM., Svistunenko, DA., Wilson, MT., Hemmings, AM., Moore, GR. and Le Brun, NE., (2020). Bacterial iron detoxification at the molecular level.. The Journal of Biological Chemistry. 295 (51), 17602-17623

Bradley, JM., Pullin, J., Moore, GR., Svistunenko, DA., Hemmings, AM. and Le Brun, NE., (2020). Routes of iron entry into, and exit from, the catalytic ferroxidase sites of the prokaryotic ferritin SynFtn.. Dalton Transactions. 49 (5), 1545-1554

Jabeen, A., Reeder, BJ., Svistunenko, D., Hisaindee, S., Ashraf, S., Al-Zuhair, S. and Battah, S., (2019). Effect of the Photodynamic Therapy Applications with Potent Microalgae Constituents on Several Types of Tumor. IRBM. 40 (1), 51-61

Adams, HR., Krewson, C., Vardanega, JE., Fujii, S., Moreno-Chicano, T., Sambongi, Y., Svistunenko, D., Paps, J., Andrew, CR. and Hough, MA., (2019). One fold, two functions: cytochrome P460 and cytochrome c′-β from the methanotroph Methylococcus capsulatus (Bath). Chemical Science. 10 (10), 3031-3041

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

Bennett, SP., Soriano-Laguna, MJ., Bradley, JM., Svistunenko, DA., Richardson, DJ., Gates, AJ. and Le Brun, NE., (2019). NosL is a dedicated copper chaperone for assembly of the CuZ center of nitrous oxide reductase. Chemical Science. 10 (19), 4985-4993

Adams, HR., Krewson, C., Vardanega, JE., Fujii, S., Moreno-Chicano, T., Sambongi, Y., Svistunenko, D., Paps, J., Andrew, CR. and Hough, MA., (2019). Correction: One fold, two functions: cytochrome P460 and cytochrome c′-β from the methanotroph Methylococcus capsulatus (Bath). Chemical Science. 10 (36), 8490-8490

Freeman, SL., Kwon, H., Portolano, N., Parkin, G., Venkatraman Girija, U., Basran, J., Fielding, AJ., Fairall, L., Svistunenko, DA., Moody, PCE., Schwabe, JWR., Kyriacou, CP. and Raven, EL., (2019). Heme binding to human CLOCK affects interactions with the E-box. Proceedings of the National Academy of Sciences. 116 (40), 19911-19916

Bradley, J., Svistunenko, D., Pullin, J., Hill, N., Stuart, R., Palenik, B., Wilson, M., Hemmings, A., Moore, G. and Le Brun, N., (2019). Reaction of O2 with a di-iron protein generates a mixed valent Fe2+/Fe3+ center and peroxide. Proceedings of the National Academy of Sciences. 116 (6), 2058-2067

Pellicer Martinez, MT., Crack, JC., Stewart, MY., Bradley, JM., Svistunenko, DA., Johnston, AW., Cheesman, MR., Todd, JD. and Le Brun, NE., (2019). Mechanisms of iron- and O₂-sensing by the [4Fe-4S] cluster of the global iron regulator RirA.. eLife. 8, e47804-

Carey, LM., Gavenko, R., Svistunenko, DA. and Ghiladi, RA., (2018). How nature tunes isoenzyme activity in the multifunctional catalytic globin Dehaloperoxidase from Amphitrite ornata. Biochimica et Biophysica Acta - Proteins and Proteomics. 1866 (2), 230-241

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

Makavitskaya, M., Svistunenko, D., Navaselsky, I., Hryvusevich, P., Mackievic, V., Rabadanova, C., Tyutereva, E., Samokhina, V., Straltsova, D., Sokolik, A., Voitsekhovskaja, O. and Demidchik, V., (2018). Novel roles of ascorbate in plants: induction of cytosolic Ca2+ signals and efflux from cells via anion channels. Journal of Experimental Botany. 69 (14), 3477-3489

Child, SA., Bradley, JM., Pukala, TL., Svistunenko, DA., Le Brun, NE. and Bell, SG., (2018). Electron transfer ferredoxins with unusual cluster binding motifs support secondary metabolism in many bacteria. Chemical Science. 9 (41), 7948-7957

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., 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

Al-Zuhair, S., Ashraf, S., Hisaindee, S., Darmaki, NA., Battah, S., Svistunenko, D., Reeder, BJ., Stanway, G. and Chaudhary, A., (2017). Enzymatic pre-treatment of microalgae cells for enhanced extraction of proteins. Engineering in Life Sciences. 17 (2), 175-185

Bradley, JM., Svistunenko, DA., Moore, GR. and Le Brun, NE., (2017). Tyr25, Tyr58 and Trp133 of: Escherichia coli bacterioferritin transfer electrons between iron in the central cavity and the ferroxidase centre. Metallomics. 9 (10), 1421-1428

Pellicer Martinez, MT., Martinez, AB., Crack, JC., Holmes, JD., Svistunenko, DA., Johnston, AWB., Cheesman, MR., Todd, JD. and Le Brun, NE., (2017). Sensing iron availability via the fragile [4Fe–4S] cluster of the bacterial transcriptional repressor RirA. Chemical Science. 8 (12), 8451-8463

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

Munnoch, JT., Martinez, MTP., Svistunenko, DA., Crack, JC., Le Brun, NE. and Hutchings, MI., (2016). Characterization of a putative NsrR homologue in Streptomyces venezuelae reveals a new member of the Rrf2 superfamily. Scientific Reports. 6 (1), 31597-

Nnamchi, CI., Parkin, G., Efimov, I., Basran, J., Kwon, H., Svistunenko, DA., Agirre, J., Okolo, BN., Moneke, A., Nwanguma, BC., Moody, PCE. and Raven, EL., (2016). Structural and spectroscopic characterisation of a heme peroxidase from sorghum. Journal of Biological Inorganic Chemistry. 21 (1), 63-70

Crack, JC., Svistunenko, DA., Munnoch, J., Thomson, AJ., Hutchings, MI. and Le Brun, NE., (2016). Differentiated, Promoter-specific Response of [4Fe-4S] NsrR DNA Binding to Reaction with Nitric Oxide. Journal of Biological Chemistry. 291 (16), 8663-8672

Sosan, A., Svistunenko, D., Straltsova, D., Tsiurkina, K., Smolich, I., Lawson, T., Subramaniam, S., Golovko, V., Anderson, D., Sokolik, A., Colbeck, I. and Demidchik, V., (2016). Engineered silver nanoparticles are sensed at the plasma membrane and dramatically modify the physiology of Arabidopsis thaliana plants. The Plant Journal. 85 (2), 245-257

Wareham, LK., Begg, R., Jesse, HE., Van Beilen, JWA., Ali, S., Svistunenko, DA., McLean, S., Hellingwerf, KJ., Sanguinetti, G. and Poole, RK., (2016). Carbon Monoxide Gas Is Not Inert, but Global, in Its Consequences for Bacterial Gene Expression, Iron Acquisition, and Antibiotic Resistance. Antioxidants & Redox Signaling. 24 (17), 1013-1028

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

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

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

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

Bradley, JM., Svistunenko, DA., Lawson, TL., Hemmings, AM., Moore, GR. and Le Brun, NE., (2015). Three Aromatic Residues are Required for Electron Transfer during Iron Mineralization in Bacterioferritin. Angewandte Chemie. 127 (49), 14976-14980

Bradley, JM., Svistunenko, DA., Lawson, TL., Hemmings, AM., Moore, GR. and Le Brun, NE., (2015). Three Aromatic Residues are Required for Electron Transfer during Iron Mineralization in Bacterioferritin. Angewandte Chemie International Edition. 54 (49), 14763-14767

Beckerson, P., Svistunenko, D. and Reeder, B., (2015). Effect of the distal histidine on the peroxidatic activity of monomeric cytoglobin. F1000Research. 4, 87-87

Silaghi-Dumitrescu, R., Svistunenko, DA., Cioloboc, D., Bischin, C., Scurtu, F. and Cooper, CE., (2014). Nitrite binding to globins: linkage isomerism, EPR silence and reductive chemistry. Nitric Oxide: Biology and Chemistry. 42, 32-39

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

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

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

Dumarieh, R., D'Antonio, J., Deliz-Liang, A., Smirnova, T., Svistunenko, DA. and Ghiladi, RA., (2013). Tyrosyl Radicals in Dehaloperoxidase. Journal of Biological Chemistry. 288 (46), 33470-33482

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)

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

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

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

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

Svistunenko, DA., Adelusi, M., Dawson, M., Robinson, P., Bernini, C., Sinicropi, A. and Basosi, R., (2011). Computation informed selection of parameters for protein radical EPR spectra simulation. Studia Universitatis Babes-Bolyai Chemia. 56 (3), 135-146

Thompson, MK., Franzen, S., Ghiladi, RA., Reeder, BJ. and Svistunenko, DA., (2010). Compound ES of Dehaloperoxidase Decays via Two Alternative Pathways Depending on the Conformation of the Distal Histidine. Journal of the American Chemical Society. 132 (49), 17501-17510

Mot, A., Zoltan, K., Svistunenko, DA., Damian, G., Silaghi-Dumitrescu, R. and Makarov, SV., (2010). ‘Super-reduced’ iron under physiologically-relevant conditions. Dalton Trans.. 39 (6), 1464-1466

Demidchik, V., Cuin, TA., Svistunenko, D., Smith, SJ., Miller, AJ., Shabala, S., Sokolik, A. and Yurin, V., (2010). Arabidopsis root K+-efflux conductance activated by hydroxyl radicals: single-channel properties, genetic basis and involvement in stress-induced cell death. Journal of Cell Science. 123 (9), 1468-1479

Demidchik, V., Cuin, TA., Svistunenko, DA., Smith, SJ., Miller, AJ., Shabala, S., Sokolik, A. and Yurin, V., (2010). Arabidopsis root K(+)-efflux conductance activated by hydroxyl radicals: single-channel properties, genetic basis and involvement in stress-induced cell death. Journal of Cell Science. 123 (9), 1468-1479

Nicholls, P., Worrall, JAR. and Svistunenko, DA., (2010). Catalatic and peroxidatic mechanisms of Mycobacterium tuberculosis catalase-peroxidase (KatG). FEBS Journal. 277 (1), creators-Svistunenko=3ADimitri_A=3A=3A

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

Svistunenko, DA. and Jones, GA., (2009). Tyrosyl radicals in proteins: a comparison of empirical and density functional calculated EPR parameters. Physical Chemistry Chemical Physics. 11 (31), 6600-6600

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

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

Chauhan, N., Basran, J., Efimov, I., Svistunenko, DA., Seward, HE., Moody, PCE. and Raven, EL., (2008). The Role of Serine 167 in Human Indoleamine 2,3-Dioxygenase: A Comparison with Tryptophan 2,3-Dioxygenase. Biochemistry. 47 (16), 4761-4769

Svistunenko, DA., Reeder, BJ., Wankasi, MM., Silaghi-Dumitrescu, R-L., Cooper, CE., Rinaldo, S., Cutruzzol?, F. and Wilson, MT., (2007). Reaction of Aplysia limacina metmyoglobin with hydrogen peroxide. Dalton Transactions (8), 840-840

Pipirou, Z., Bottrill, AR., Svistunenko, DA., Efimov, I., Basran, J., Mistry, SC., Cooper, CE. and Raven, EL., (2007). The Reactivity of Heme in Biological Systems:  Autocatalytic Formation of Both Tyrosine−Heme and Tryptophan−Heme Covalent Links in a Single Protein Architecture. Biochemistry. 46 (46), 13269-13278

Svistunenko, DA., Davies, N., Brealey, D., Singer, M. and Cooper, CE., (2006). Mitochondrial dysfunction in patients with severe sepsis: An EPR interrogation of individual respiratory chain components. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1757 (4), 262-272

Cooper, CE., Jurd, M., Nicholls, P., Wankasi, MM., Svistunenko, DA., Reeder, BJ. and Wilson, MT., (2005). On the formation, nature, stability and biological relevance of the primary reaction intermediates of myoglobins with hydrogen peroxide. Dalton Transactions (21), 3483-3483

Davies, NA., Brealey, DA., Stidwill, R., Singer, M., Svistunenko, DA. and Cooper, CE., (2005). Nitrosyl heme production compared in endotoxemic and hemorrhagic shock. Free Radical Biology and Medicine. 38 (1), 41-49

Papadopoulou, ND., Mewies, M., McLean, KJ., Seward, HE., Svistunenko, DA., Munro, AW. and Raven, EL., (2005). Redox and Spectroscopic Properties of Human Indoleamine 2,3-Dioxygenase and A His303Ala Variant:  Implications for Catalysis. Biochemistry. 44 (43), 14318-14328

Kagan, VE., Tyurin, VA., Jiang, J., Tyurina, YY., Ritov, VB., Amoscato, AA., Osipov, AN., Belikova, NA., Kapralov, AA., Kini, V., Vlasova, II., Zhao, Q., Zou, M., Di, P., Svistunenko, DA., Kurnikov, IV. and Borisenko, GG., (2005). Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors. Nature Chemical Biology. 1 (4), 223-232

Svistunenko, DA., (2005). Reaction of haem containing proteins and enzymes with hydroperoxides: The radical view. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1707 (1), 127-155

Silkstone, GG., Cooper, CE., Svistunenko, D. and Wilson, MT., (2005). EPR and Optical Spectroscopic Studies of Met80X Mutants of Yeast Ferricytochrome c. Models for Intermediates in the Alkaline Transition. Journal of the American Chemical Society. 127 (1), 92-99

Carlsson, GH., Nicholls, P., Svistunenko, D., Berglund, GI. and Hajdu, J., (2005). Complexes of Horseradish Peroxidase with Formate, Acetate, and Carbon Monoxide. Biochemistry. 44 (2), 635-642

Reeder, BJ., Svistunenko, DA., Cooper, CE. and Wilson, MT., (2004). The Radical and Redox Chemistry of Myoglobin and Hemoglobin: From In Vitro Studies to Human Pathology. Antioxidants & Redox Signaling. 6 (6), 954-966

Svistunenko, DA., Wilson, MT. and Cooper, CE., (2004). Tryptophan or tyrosine? On the nature of the amino acid radical formed following hydrogen peroxide treatment of cytochrome c oxidase. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1655 (1-3), 372-380

Svistunenko, DA. and Cooper, CE., (2004). A New Method of Identifying the Site of Tyrosyl Radicals in Proteins. Biophysical Journal. 87 (1), 582-595

Reeder, BJ., Svistunenko, DA., Cooper, CE. and Wilson, MT., (2004). The Radical and Redox Chemistry of Myoglobin and Hemoglobin: From<I> In Vitro</I> Studies to Human Pathology. Antioxidants and Redox Signaling. 6 (6), 954-966

Vanin, AF., Svistunenko, DA., Mikoyan, VD., Serezhenkov, VA., Fryer, MJ., Baker, NR. and Cooper, CE., (2004). Endogenous Superoxide Production and the Nitrite/Nitrate Ratio Control the Concentration of Bioavailable Free Nitric Oxide in Leaves. Journal of Biological Chemistry. 279 (23), 24100-24107

Malone, SA., Lewin, A., Kilic, MA., Svistunenko, DA., Cooper, CE., Wilson, MT., Le Brun, NE., Spiro, S. and Moore, GR., (2004). Protein-Template-Driven Formation of Polynuclear Iron Species. Journal of the American Chemical Society. 126 (2), 496-504

(2004). Correction. Biophysical Journal. 87 (5), 3614-3616

Svistunenko, DA., Reeder, BJ., Wilson, MT. and Cooper, CE., (2003). Radical Formation and Migration in Myoglobins. Progress in Reaction Kinetics and Mechanism. 28 (1), 105-118

Murphy, MP., Echtay, KS., Blaikie, FH., Asin-Cayuela, J., Cochemé, HM., Green, K., Buckingham, JA., Taylor, ER., Hurrell, F., Hughes, G., Miwa, S., Cooper, CE., Svistunenko, DA., Smith, RAJ. and Brand, MD., (2003). Superoxide Activates Uncoupling Proteins by Generating Carbon-centered Radicals and Initiating Lipid Peroxidation. Journal of Biological Chemistry. 278 (49), 48534-48545

McHugh, JP., Rodríguez-Quiñones, F., Abdul-Tehrani, H., Svistunenko, DA., Poole, RK., Cooper, CE. and Andrews, SC., (2003). Global Iron-dependent Gene Regulation in Escherichia coli. Journal of Biological Chemistry. 278 (32), 29478-29486

Svistunenko, DA., Dunne, J., Fryer, M., Nicholls, P., Reeder, BJ., Wilson, MT., Bigotti, MG., Cutruzzolà, F. and Cooper, CE., (2002). Comparative Study of Tyrosine Radicals in Hemoglobin and Myoglobins Treated with Hydrogen Peroxide. Biophysical Journal. 83 (5), 2845-2855

Reeder, BJ., Svistunenko, DA., Sharpe, MA. and Wilson, MT., (2002). Characteristics and Mechanism of Formation of Peroxide-Induced Heme to Protein Cross-Linking in Myoglobin. Biochemistry. 41 (1), 367-375

Torres, J., Svistunenko, D., Karlsson, B., Cooper, CE. and Wilson, MT., (2002). Fast Reduction of a Copper Center in Laccase by Nitric Oxide and Formation of a Peroxide Intermediate. Journal of the American Chemical Society. 124 (6), 963-967

Svistunenko, DA., (2001). An EPR study of the peroxyl radicals induced by hydrogen peroxide in the haem proteins. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1546 (2), 365-378

SVISTUNENKO, DA., SHARPE, MA., NICHOLLS, P., BLENKINSOP, C., DAVIES, NA., DUNNE, J., WILSON, MT. and COOPER, CE., (2000). The pH dependence of naturally occurring low-spin forms of methaemoglobin and metmyoglobin: an EPR study. Biochemical Journal. 351 (3), 595-605

Svistunenko, DA., Sharpe, MA., Nicholls, P., Wilson, MT. and Cooper, CE., (2000). A New Method for Quantitation of Spin Concentration by EPR Spectroscopy: Application to Methemoglobin and Metmyoglobin. Journal of Magnetic Resonance. 142 (2), 266-275

Silver, J., Marsh, PJ., Symons, MCR., Svistunenko, DA., Frampton, CS. and Fern, GR., (2000). Crystal Structure of Bis(4-methylimidazole)tetraphenylporphyrinatoiron(III) Chloride and Related Compounds. Correlation of Ground State with Fe−N Bond Lengths. Inorganic Chemistry. 39 (13), 2874-2881

Silver, J., Marsh, PJ., Symons, MCR., Svistunenko, DA., Frampton, CS. and Fern, GR., (2000). Crystal structure of bis(4-methylimidazole) tetraphenylporphyrinatoiron(III) chloride and related compounds. Correlation of ground state with Fe-N bond lengths. INORGANIC CHEMISTRY. 39 (13), 2874-2881

SVISTUNENKO, DA., SHARPE, MA., NICHOLLS, P., BLENKINSOP, C., DAVIES, NA., DUNNE, J., WILSON, MT. and COOPER, CE., (2000). The pH dependence of naturally occurring low-spin forms of methaemoglobin and metmyoglobin: an EPR study. Biochemical Journal. 351 (3), 595-595

Svistunenko, DA., Rob, A., Ball, A., Torres, J., Symons, MCR., Wilson, MT. and Cooper, CE., (1999). The electron paramagnetic resonance characterisation of a copper-containing extracellular peroxidase from Thermomonospora fusca BD25. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1434 (1), 74-85

Dunne, J., Svistunenko, DA., Wilson, MT., Alayash, AI. and Cooper, CE., (1998). Reactions of cross-linked ferric haemoglobins with hydrogen peroxide. Biochemical Society Transactions. 26 (4), 9-15

Dunne, J., Svistunenko, DA., Wilson, MT., Alayash, AI. and Cooper, CE., (1998). 20 Reactions of cross-linked ferric haemoglobins with hydrogen peroxide. Biochemical Society Transactions. 26 (4), S320-S320

Cooper, CE., Torres, J., Sharpe, MA., Wilson, MT. and Svistunenko, DA., (1998). Peroxynitrite Reacts with Methemoglobin to Generate Globin-Bound Free Radical Species. Advances in Experimental Medicine and Biology. 454, 195-202

Moore, KP., Holt, SG., Patel, RP., Svistunenko, DA., Zackert, W., Goodier, D., Reeder, BJ., Clozel, M., Anand, R., Cooper, CE., Morrow, JD., Wilson, MT., Darley-Usmar, V. and Roberts, LJ., (1998). A Causative Role for Redox Cycling of Myoglobin and Its Inhibition by Alkalinization in the Pathogenesis and Treatment of Rhabdomyolysis-induced Renal Failure. Journal of Biological Chemistry. 273 (48), 31731-31737

Svistunenko, DA., Patel, RP., Voloshchenko, SV. and Wilson, MT., (1997). The Globin-based Free Radical of Ferryl Hemoglobin Is Detected in Normal Human Blood. Journal of Biological Chemistry. 272 (11), 7114-7121

PATEL, RP., SVISTUNENKO, D., WILSON, MT. and DARLEY-USMAR, VM., (1997). Reduction of Cu(II) by lipid hydroperoxides: implications for the copper-dependent oxidation of low-density lipoprotein. Biochemical Journal. 322 (2), 425-433

Svistunenko, DA., Patel, RP. and Wilson, MT., (1996). An EPR Investigation of Human Methaemoglobin Oxidation by Hydrogen Peroxide: Methods to Quantify all Paramagnetic Species Observed in the Reaction. Free Radical Research. 24 (4), 269-280

Patel, RP., Svistunenko, DA., Darley-usmar, VM., Symons, MCR. and Wilson, MT., (1996). Redox Cycling of Human Methaemoglobin by H₂O₂Yields Persistent Ferryl Iron and Protein Based Radicals. Free Radical Research. 25 (2), 117-123

Symons, MCR., Taiwo, FA. and Svistunenko, DA., (1993). Electron paramagnetic resonance studies of hole mobility and localisation in haemoglobin. Journal of the Chemical Society, Faraday Transactions. 89 (16), 3071-3071

Boulton, M., Dontsov, A., Jarvis-Evans, J., Ostrovsky, M. and Svistunenko, D., (1993). Lipofuscin is a photoinducible free radical generator. Journal of Photochemistry and Photobiology B: Biology. 19 (3), 201-204

Svistunenko, DA., (1991). The decomposition of the EPR spectra of multicomponent systems irradiated at 77 K into paramagnetic center signals of different natures. Izevestiya Akademii Nauk SSSR - Seriya Biologicheskaya (4), 540-557

SVISTUNENKO, DA., (1991). THE DECOMPOSITION OF AN EPR-SPECTRUM OF A MULTICOMPONENT SYSTEM, IRRADIATED AT 77-K, INTO DIFFERENT PARAMAGNETIC CENTER SIGNALS. IZVESTIYA AKADEMII NAUK SSSR SERIYA BIOLOGICHESKAYA (4), 540-557

Svistunenko, DA., (1990). [Ascorbic acid radicals induced by the action of radiation in tissues from rat organs frozen at 77 K].. Izvestiia Akademii nauk SSSR. Seriia biologicheskaia (6), 827-834

Svistunenko, DA., (1990). Ascorbic acid radicals induced by radiation in frozen at 77 K rat tissues. Izevestiya Akademii Nauk SSSR - Seriya Biologicheskaya (6), 827-834

Svistunenko, DA. and Gudtsova, KV., (1989). Modification by cystamine of radiation-induced free radical damages to biomolecules in tissues of mouse organs. Radiobiologiya. 29 (1), 3-7

JURCZYK, MU., SVISTUNENKO, DA., KUDRYAVTSEV, ME. and KUROPTEVA, ZV., (1989). ASCORBIC-ACID RADICALS INDUCED BY RADIATION IN TUMOR-TISSUES. STUDIA BIOPHYSICA. 133 (1), 19-24

Svistunenko, DA., Kosaganova, NI. and Kopylovskiĭ, SA., (1986). [Paramagnetic centers formed in mouse blood gamma-irradiated at 77K].. Radiobiologiia. 26 (1), 28-34

Svistunenko, DA., Rikhireva, GT. and Pulatova, MK., (1986). Radiation-induced free radicals of DNA, DNA content in tissues, and tissue radiosensitivity. Radiobiologiya. 26 (1), 22-27

Svistunenko, DA., Kosaganova Yu., N. and Kopylovsky, SA., (1986). Paramagnetic centres formed in mouse blood after γ-irradiation at 77 K. Radiobiologiya. 26 (1), 28-34

Svistunenko, DA., Rikhireva, GT., Pulatova, MK. and Ermakov, VM., (1984). Free-radical disorders in the tissues of mice exposed to gamma irradiation and neutrons in vitro. The radiochemical yields. Radiobiologiya. 24 (1), 3-8

A. Svistunenko, D., A. Davies, N., T. Wilson, M., P. Stidwill, R., Singer, M. and E. Cooper, C., (1997). Free radical in blood: a measure of haemoglobin autoxidation in vivo? †