Reeder, Brandon - University of Essex - School of Biological Sciences

个人简介

2011-Present Lecturer of Biochemistry and Molecular Biophysics, Department of Biological Sciences, University of Essex, UK. 2008-2010 Senior Research Officer, Department of Biological Sciences, University of Essex, UK. BBSRC funded research project: “Formation of Tyrosine Radicals in haem proteins: their role in electron transfer” 2006-2007 Senior Research Officer, Department of Biological Sciences, University of Essex, UK. EU Framework VI funded multi-centre academic and industrial European team: “Genomics and Blood Substitutes for 21st Century Europe” 2003-2006 Senior Research Officer, Department of Biological Sciences, University of Essex, UK. BBSRC funded research project: “Characterisation of haem-protein cross-linked respiratory proteins: investigation of mechanisms for enhanced pro-oxidant activity”. 1999 – 2003 Senior Research Officer, Department of Biological Sciences, University of Essex, UK. Wellcome Trust funding research project: “Molecular mechanisms of haem-protein induced oxidative injury: Rhabdomyolysis-induced renal failure”.

研究领域

Biochemical and Biomedical based-research, particularly in the role of proteins in health and disease. Some of my current research focuses on metalloproteins in health and disease: The next generation of blood substitutes (see www.haemO2.com) Role of human cytoglobin in lipid binding, lipid oxidation, cell signalling and cancer therapy resistance. Role of neuroglobin in cell signalling and cell protection in neurodegenerative diseases such as Alzheimer’s. Biochemical mechanisms oxidative stress in acute renal failure following rhabdomyolysis and delayed vasospasm following subarachnoid haemorrhage. Structure and functional roles of non-symbiotic plant haemoglobins and bacterial globins. Cell signalling by oxidatively modified lipids and formation of singlet oxygen resulting from lipid oxidation. Developing novel compounds as ameliorators of haemoprotein-induced oxidative reactions.

近期论文

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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 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 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 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 Beckerson, P., Svistunenko, D.A., Reeder B.J., “Effect of the distal histidine on the peroxidatic activity of monomeric cytoglobin” Accepted F1000 research 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 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 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 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 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. 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 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 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 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 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 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 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 Wilson, M.T. & Reeder, B.J. “Oxygen binding haem proteins” Exp. Physiol. (2008) 93(1) 128-132 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 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