Publications List

Original Articles and Reviews

  1. Villar,I, Larrainzar, E., Milazzo, L., Pérez-Rontomé C., Rubio, M.C., Smulevich, G., Martínez, G.I., Wilson, M.T., Reeder, B.J., Huertas, R., Abbruzzetti, S., Udvardi, M., Becana, M. “A Plant Gene Encoding One-Heme and Two-Heme Hemoglobins with Extreme Reactivities Towards Diatomic Gases and Nitrite” Front. Plant Sci.(2020)  11, 1743-1757

  2. Cooper, C.E., Silkstone, G. G. A., Simons, M., Gretton, S. Rajagopal, B. S., Allen-Baume, V., Syrett, N. Shaik, T., Popa, G., Sheng, X., Bird, M., Choi, JW., Piano, R., Ronda, L.,  Betatti, S., Paredi, G., Mozzarelli, A., Reeder, B. J “Engineering hemoglobin to enable homogenous PEGylation without modifying protein functionality” Biomater. Sci. (2020) 8, 3896-3906

  3. Leiva-Eriksson, N., Reeder, B. J., Wilson, M.T. and Bülow, L. “Sugar beet hemoglobins: reactions with nitric oxide and nitrite reveal differential roles for nitrogen metabolism” Biochem J. (2019) 476, 2111-2125

  4. Cooper, C.E., Silkstone, G. G. A., Simons, M., Rajagopal, B. S., Syrett, N. Shaik, T., Gretton, S. Welbourn, E., Bulow, L., Leiva-Eriksson, N.,  Ronda, L.,  Mozzarelli, A., Eke, A., Mathe, D. Reeder, B. J., “Engineering tyrosine residues into hemoglobin enhances heme reduction, decreases oxidative stress and increases vascular retention of a hemoglobin based blood substitute” Free Rad. Biol. Med. (2019) 134, 106-118

  5. Silkstone, G. G. A., Simons, M., Rajagopal, B. S., Shaik, T., Reeder, B. J., and Cooper, C. E. “Novel Redox Active Tyrosine Mutations Enhance the Regeneration of Functional Oxyhemoglobin from Methemoglobin: Implications for Design of Blood Substitutes”. Adv. Exp. Med. Biol. (2018)1072, 221-225.

  6. Simons, M., Gretton, S., Silkstone, G.G.A, Rajagopal, B.S., Allen-Baume, V., Syrett, N., Shaik, T., Eriksson, N., Ronda, L., Mozzarelli, A., Strader, M.B., Alayash, A.I., Reeder, B.J. & Cooper, C.E. “Comparison of the oxidative reactivity of recombinant fetal and adult human hemoglobin: implications for the design of hemoglobin-based oxygen carriers” Bioscience Reports. Bioscience Reports.(2018) 38, 1-19.

  7. Alomari, E., Ronda, L., Bruno, S., Paredi, G., Marchetti, M., Bettati, S., Olivari, D., Fumagalli,F.,  Novelli, D., Ristagno G., Latini, R. Cooper, C.E., Reeder, B.J., Mozzarelli, A. “High- and low-affinity PEGylated hemoglobin-based oxygen carriers: differential oxidative stress in a Guinea pig transfusion model” Free Rad. Biol. Med. (2018) 124, 299-310

  8. Reeder, B.J., Ukeri, J. “Strong modulation of nitrite reductase activity of cytoglobin by disulfide bond oxidation: Implications for nitric oxide homeostasis” Nitric Oxide (2018) 72, 16-23

  9. Reeder, B.J. Forum Review: “Redox and peroxidase activities of the hemoglobin superfamily - relevancy to health and disease.” Antioxid. Redox. Sign. (2017) 26(14) 763-776

  10. Jabeen, A., AlDarmaki, N. Hisaindee, S. Reeder, B.J. Salman, S. “Effect of Enzymatic Pre-treatment of Microalgae Extracts on their Anti-tumor Activity” Biomed J. (2017) In Press

  11. Vos, M.H., Reeder, B.J. Daldalc, F. and Liebla, U. “Ultrafast photochemistry of the bc1 complex” Phys. Chem. Chem. Phys. (2017) 19, 6807–6813

  12. Silkstone, G., Silkstone, R.S., Wilson, M.T., Simons, M., Bulow, L., Kallberg, K., Ratanaspo, K., Ronda, L., Mozzarelli, A., Reeder, B.J., Cooper, C.E. “Engineering tyrosine electron transfer pathways decreases oxidative toxicity in hemoglobin: implications for blood substitute design” Biochem J. (2016) 473, 3371-3383

  13. Al-Zuhair, S., Ashraf, S., Hisaindee, S., Al Darmaki, N., Battah, S., Svistunenko, D, Reeder, B.  Stanway, G., Chaudhary, A. “Enzymatic Pre-treatment of Microalgae Cells for Enhanced Extraction of Proteins” Eng. Life Sci. (2016) 17­, 175-185

  14. Silkstone, R.S., Silkstone, G., Baath, J.A., Rajagopal, B., Nicholls, P., Reeder, B.J., Ronda, L., Bulow, L., Cooper, C.E. “The betaLys66Tyr Variant of Human Hemoglobin as a Component of a Blood Substitute.” Adv. Exp. Med. Biol. (2016) 876, 455-460

  15. Beckerson, P., Wilson, M.T., Svistunenko, D.A., Reeder B.J. “Cytoglobin ligand binding regulated by changing haem-coordination in response to intramolecular disulfide bond formation and lipid interaction” Biochem. J. (2015) 465, 127-137

  16. Beckerson, P., Reeder B.J., Wilson, M.T., “Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding” FEBS Lett (2015) 589, 507-512

  17. Zhu C.F., Battah S., Kong X., Reeder B.J., Hider R.C., Zhou T. “Design, synthesis and biological evaluation of 5-aminolaevulinic acid/3-hydroxypyridinone conjugates as potential photodynamic therapeutical agents.” Bioorg. Med Chem Lett. (2015) 25, 1750-1756

  18. Beckerson, P., Svistunenko, D.A., Reeder B.J., “Effect of the distal histidine on the peroxidatic activity of monomeric cytoglobin” F1000 research (2015) 4, 87

  19. Reeder B.J., Hough M.A. “The crystal structure of class 3 non-symbiotic plant hemoglobin from Arabidopsis thaliana reveals a novel N-terminal helical extension” Acta Cryst. (2014) D70, 1411-1418

  20. Ascenzi P., Marino M., Polticelli F., Coletta M., Gioia M., Marini S., Pesce A., Nardini M., Bolognesi M., Reeder B.J., Wilson M.T. “Non-covalent and covalent modifications modulate the reactivity of monomeric mammalian globins” Biochim. Biophys. Acta (2013) 1834, 1750-1756

  21. Cooper, C.E., Schaer, D., Buehler, P.W., Wilson, M.T.,  Reeder, B.J., Silkstone, G.,  Svistunenko, D.A., Bulow, L., and  Alayash, A. "Haptoglobin binding stabilizes hemoglobin ferryl iron and the globin radical on tyrosine beta-145"   Antioxidants & Redox Signaling  (2013) 18, 2246-2273

  22. Wankasi, M.M., Reeder, B.J. and Wilson, M.T. “Studies on the reactions of hydrogen peroxide with Sickle cell haemoglobin” Sky J. Biochem. Res. (2013) 2, 27-36

  23. Reeder B.J., Svistunenko D.A. Cooper, C.E. and Wilson M.T. “Engineering tyrosine-based electron flow pathways in proteins: the case of Aplysia myoglobin” J. Am. Chem Soc. (2012) 134, 7741-7749.

  24. Reeder B.J., Svistunenko D.A. and Wilson M.T. “Lipid binding to cytoglobin leads to a change in heme coordination: a role for cytoglobin in lipid signalling of oxidative stress” Biochem. J. (2011) 434(3), 483-492

  25. Thompson, M., Stefan, F., Reza, G., Reeder B.J. and Svistunenko, D.A., “Compound ES of dehaloperoxidase decays via two alternative pathways depending on the conformation of the distal histidine” J. Am. Chem Soc. (2010), 132(49), 17501–17510

  26. Boutaud, O., Moore K.P., Reeder B.J., Harry D., Howie A.J., Wang, S., Carney C.K., Mastersona T.S., Amin T., Wright, D.W., Wilson M.T., Oates J.A. and Roberts L.J. “Acetaminophen inhibits hemoprotein-catalyzed lipid peroxidation and attenuates rhabdomyolysis-induced renal failure” Proc Natl Acad Sci USA (2010) 107(6), 2699-2704

  27. Reeder, B.J. Comprehensive Invited Review: “The redox activity of hemoglobins: From physiological functions to pathologic mechanisms.” Antioxid. Redox. Sign. (2010) 13(7) 1087-1123

  28. Gaucher-Di Stasio, C., Paternotte, E., Prin-Mathieuc, C., Reeder, B.J., Poitevin, G., Labrude, P., Stoltz,  J., Copper, C.E., Menu, P. ”The importance of the effect of shear stress on endothelial cells in determining the performance of hemoglobin based oxygen carriers” Biomaterials (2009) 30(4), 445-451

  29. Reeder, B.J., Grey, M., Silaghi-Dumitrescu, R., Svistunenko, D.A., Bülow, L., Cooper, C.E. & Wilson, M.T “Tyrosine residues as redox cofactors in human hemoglobin: Implications for engineering non toxic blood substitutes” J. Biol. Chem (2008) 283(45), 30780-30787

  30. Reeder, B.J., Hider, R.C. & Wilson, M.T “Iron chelators can protect against oxidative stress through ferryl heme reduction” Free Rad. Biol. Med.(2008) 44(3) 264-273

  31. Reeder, B.J., Cutruzzola, F., Bigotti, M.  Hider, R.C. & Wilson, M.T “Tyrosine as a redox-active center in electron transfer to ferryl heme in globins” Free Rad. Biol. Med. (2008) 44(3) 274-283

  32. Wilson, M.T. & Reeder, B.J. “Oxygen binding haem proteins” Exp. Physiol. (2008) 93(1) 128-132

  33. Reeder, B.J., Cutruzzolà, F., Bigotti, M.G., Watmough, N.J., & Wilson M.T. “Histidine and not tyrosine is required for the peroxide-induced formation of haem to protein cross-linked myoglobin.” IUBMB Life (2007) 59(8) 477-489

  34. Svistunenko, D.A., Reeder, B.J., Wankasi M.M., Silaghi-Dumitrescu, R., Cooper, C.E., Rinaldo, S, Cutruzzolà, F. & Wilson, M.T. “Reaction of Aplysia limacina Metmyoglobin with Hydrogen Peroxide”. Dalton Trans (2007) 8, 840-850

  35. Silaghi-Dumitrescu, R., Reeder, B.J., Nicholls, P., Cooper, C.E. & Wilson, M.T. “Ferryl haem protonation gates peroxidatic reactivity in globins” Biochem. J. (2007) 403(3), 391–395

  36. Flors, C., Fryer, M. J., Waring, J., Reeder, B.J., Bechtold, U., Mullineaux, P. M., Nonell, S., Wilson, M. T., Baker, N. R. “Imaging the production of singlet oxygen in vivo using a new fluorescent sensor, Singlet Oxygen Sensor Green®” J. Exp. Bot. (2006) 57(8), 1725-1734

  37. Reeder, B.J. & Wilson, M.T. “Desferrioxamine inhibits production of cytotoxic heme to protein cross-linked myoglobin: A mechanism to protect against oxidative stress without iron chelation” Chem. Res. Toxicol (2005) 18(6), 1004-1011

  38. Reeder, B.J. & Wilson, M.T. “Hemoglobin and myoglobin associated oxidative stress: from molecular mechanisms to disease states” Current Med. Chem. (2005) 12(23), 2741-2751

  39. Cooper, C.E., Jurd, M., Nicholls, P., Wankasi, M.M., Svistunenko, D.A., Reeder, B.J. and Wilson, M.T. “On the formation, nature, stability and biological relevance of the primary reaction intermediates of myoglobins with hydrogen peroxide” Dalton Trans (2005) 21, 3483-3488

  40. Vollaard, N.B., Reeder, B.J., Shearman, J.P., Menu, P., Wilson, M.T., Cooper, C.E. “A new sensitive assay reveals that hemoglobin is oxidatively modified in vivo” Free Rad. Biol. Med (2005) 39(9), 1216-1228

  41. Reeder, B.J., Svistunenko, D.A., Cooper, C.E., and Wilson, M.T. “The radical and redox chemistry of myoglobin and hemoglobin: From in vitro studies to human pathology”. Antioxid. Redox. Sign. (2004) 6(6), 954-966

  42. Svistunenko, D.A., Reeder, B.J., Wilson, M.T. and Cooper, C.E. “Radical formation and migration in myoglobins”. Prog. React. Kin. Mech. (2003) 28, 105-118

  43. Svistunenko, D., Dunne, J., Fryer, M., Nicholls, P., Reeder, B. J., Wilson, M., Bigotti, M. Cutruzzolà, F. and Cooper, C. “A comparative study of tyrosine radicals in hemoglobin and myoglobins treated with hydrogen peroxide” Biophys. J. (2002) 83(5), 2845-2855

  44. Reeder, B.J., Sharpe, M.A., Kay, A.D., Kerr, M.D., Moore, K. and Wilson, M.T. “Toxicity of Myoglobin and Haemoglobin: Oxidative stress in patients with Rhabdomyolysis and Subarachnoid Haemorrhage.” Biochem. Soc. Trans. (2002) 30(4), 745-748.

  45. Reeder, B.J., Svistunenko, D. A., Sharpe, M and Wilson, M.T. “Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin” Biochemistry (2002) 41(1), 367-375

  46. Mason, M.G., Ball, A.S., Reeder, B.J., Silkstone, G., Nicholls, P. and Wilson, M.T. “Extracellular Heme Peroxidases in Actinomycetes: a Case of Mistaken Identity” Appl. Environ. Microbio. (2001) 67(10), 4512-4519

  47. Reeder, B.J. and Wilson, M.T. “The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: A role for the protonated ferryl species” Free Rad. Biol. Med.  (2001) 30(11), 1311-1318

  48. Holt, S., Reeder, B.J., Wilson, M.T., Harvey, S., Morrow, J.D., Roberts, L.J. and Moore, K.P. "Increased lipid peroxidation in patients with rhabdomyolysis" The Lancet (1999) 353(9160), 1241

  49. Moore K.P., Holt S., Patel R.P., Svistunenko D.A., Zackert W. Goodier, D., Reeder B.J., Clozel M., Anand R., Cooper C.E., Morrow J.D., Wilson M.T., Darley-Usmar V. & Roberts L.J. “A causative role for redox cycling of myoglobin and its inhibition by alkalinisation in the treatment of Rhabdomyolysis-Induced Renal Failure” J. Biol. Chem. (1998) 273(48), 31731–31737

  50. Reeder, B.J. & Wilson, M.T. “Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoic acid” Biochem. J. (1998) 330(3), 1317-1323

  51. Rogers, M.S., Patel, R.P., Reeder, B.J, Sarti, P., Wilson, M.T. & Alayash, A.I. “Pro-oxidant effects of cross-linked haemoglobins explored using liposome and cytochrome c oxidase vesicle model membranes” Biochem. J.  (1995) 318(3), 827-833


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