Publications List
Original Articles and Reviews
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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
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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
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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
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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
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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.
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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.
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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.
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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
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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
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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
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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
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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
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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
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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
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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
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Wilson, M.T. & Reeder, B.J. “Oxygen binding haem proteins” Exp. Physiol. (2008) 93(1) 128-132
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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.
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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
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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
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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
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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
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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
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Reeder, B.J. & Wilson, M.T. “Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoic acid” Biochem. J. (1998) 330(3), 1317-1323
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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