Dr Brandon Reeder

Reeder, BJ., (2023). Insights into the function of cytoglobin.. Biochemical Society Transactions. 51 (5), 1907-1919

Wilson, MT. and Reeder, BJ., (2022). The peroxidatic activities of Myoglobin and Hemoglobin, their pathological consequences and possible medical interventions.. Molecular Aspects of Medicine. 84, 101045-101045

Ukeri, J., Wilson, MT. and Reeder, BJ., (2022). Modulating Nitric Oxide Dioxygenase and Nitrite Reductase of Cytoglobin through Point Mutations.. Antioxidants. 11 (9), 1816-1816

Villar, I., Larrainzar, E., Milazzo, L., Pérez-Rontomé, C., Rubio, MC., Smulevich, G., Martínez, JI., Wilson, MT., Reeder, B., Huertas, R., Abbruzzetti, S., Udvardi, M. and Becana, M., (2021). Corrigendum: A Plant Gene Encoding One-Heme and Two-Heme Hemoglobins With Extreme Reactivities Toward Diatomic Gases and Nitrite. Frontiers in Plant Science. 11

Cooper, CE., Bird, M., Sheng, X., Choi, J-W., Silkstone, GGA., Simons, M., Syrett, N., Piano, R., Ronda, L., Bettati, S., Paredi, G., Mozzarelli, A. and Reeder, BJ., (2021). Stability of Maleimide-PEG and Mono-Sulfone-PEG Conjugation to a Novel Engineered Cysteine in the Human Hemoglobin Alpha Subunit. Frontiers in Chemistry. 9, 707797-

Villar, I., Rubio, MC., Calvo-Begueria, L., Pérez-Rontomé, C., Larrainzar, E., Wilson, MT., Sandal, N., Mur, LA., Wang, L., Reeder, B., Duanmu, D., Uchiumi, T., Stougaard, J. and Becana, M., (2021). Three classes of hemoglobins are required for optimal vegetative and reproductive growth of Lotus japonicus: genetic and biochemical characterization of LjGlb2-1. Journal of Experimental Botany. 72 (22), 7778-7791

Cooper, CE., Silkstone, GGA., Simons, M., Gretton, S., Rajagopal, BS., Allen-Baume, V., Syrett, N., Shaik, T., Popa, G., Sheng, X., Bird, M., Choi, J-W., Piano, R., Ronda, L., Bettati, S., Paredi, G., Mozzarelli, A. and Reeder, BJ., (2020). Engineering hemoglobin to enable homogenous PEGylation without modifying protein functionality. Biomaterials Science. 8 (14), 3896-3906

Villar, I., Larrainzar, E., Milazzo, L., Pérez-Rontomé, C., Rubio, MC., Smulevich, G., Martínez, JI., Wilson, MT., Reeder, B., Huertas, R., Abbruzzetti, S., Udvardi, M. and Becana, M., (2020). A Plant Gene Encoding One-Heme and Two-Heme Hemoglobins With Extreme Reactivities Toward Diatomic Gases and Nitrite. Frontiers in Plant Science. 11

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

Cooper, CE., Silkstone, GGA., Simons, M., Rajagopal, B., Syrett, N., Shaik, T., Gretton, S., Welbourn, E., Bülow, L., Eriksson, NL., Ronda, L., Mozzarelli, A., Eke, A., Mathe, D. and Reeder, BJ., (2019). Engineering tyrosine residues into hemoglobin enhances heme reduction, decreases oxidative stress and increases vascular retention of a hemoglobin based blood substitute. Free Radical Biology and Medicine. 134, 106-118

Leiva Eriksson, N., Reeder, BJ., Wilson, MT. and Bülow, L., (2019). Sugar beet hemoglobins: reactions with nitric oxide and nitrite reveal differential roles for nitrogen metabolism. Biochemical Journal. 476 (14), 2111-2125

Reeder, BJ. and Ukeri, J., (2018). Strong modulation of nitrite reductase activity of cytoglobin by disulfide bond oxidation: Implications for nitric oxide homeostasis. Nitric Oxide: Biology and Chemistry. 72, 16-23

Simons, M., Gretton, S., Silkstone, GG., Rajagopal, BS., Allen-Baume, V., Syrett, N., Shaik, T., Eriksson, N., Ronda, L., Mozzarelli, A., Strader, MB., Alayash, AI., Reeder, BJ. and Cooper, CE., (2018). Comparison of the oxidative reactivity of recombinant fetal and adult human hemoglobin: implications for the design of hemoglobin-based oxygen carriers.. Bioscience Reports. 38 (4), BSR20180370-

Alomari, EAM., Ronda, L., Bruno, S., Paredi, G., Marchetti, M., Bettati, S., Olivari, D., Fumagalli, F., Novelli, D., Ristagno, G., Latini, R., Cooper, CE., Reeder, BJ. and Mozzarelli, A., (2018). High- and low-affinity PEGylated hemoglobin-based oxygen carriers: differential oxidative stress in a Guinea pig transfusion model. Free Radical Biology and Medicine. 124, 299-310

Reeder, BJ., (2017). Redox and Peroxidase Activities of the Hemoglobin Superfamily: Relevance to Health and Disease. Antioxidants & Redox Signaling. 26 (14), 763-776

Vos, MH., Reeder, BJ., Daldal, F. and Liebl, U., (2017). Ultrafast photochemistry of the bc₁ complex. Physical Chemistry Chemical Physics. 19 (9), 6807-6813

Vos, MH., Reeder, BJ., Daldal, F. and Liebl, U., (2017). Correction: Ultrafast photochemistry of the bc₁ complex. Physical Chemistry Chemical Physics. 19 (13), 9320-9320

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

Jabeen, A., Reeder, B., Hisaindee, S., Ashraf, S., Darmaki, NA., Battah, S. and Al-Zuhair, S., (2017). Effect of Enzymatic pre-treatment of microalgae extracts on their anti-tumor activity. Biomedical Journal. 40 (6), 339-346

Silkstone, RS., Silkstone, G., Baath, JA., Rajagopal, B., Nicholls, P., Reeder, BJ., Ronda, L., Bulow, L. and Cooper, CE., (2016). The βLys66Tyr Variant of Human Hemoglobin as a Component of a Blood Substitute. Advances in Experimental Medicine and Biology. 876, 455-460

Silkstone, GGA., Silkstone, RS., Wilson, MT., Simons, M., Bülow, L., Kallberg, K., Ratanasopa, K., Ronda, L., Mozzarelli, A., Reeder, BJ. and Cooper, CE., (2016). Engineering tyrosine electron transfer pathways decreases oxidative toxicity in hemoglobin: implications for blood substitute design. Biochemical Journal. 473 (19), 3371-3383

Zhou, T., Shao, L-L., Battah, S., Zhu, C-F., Hider, RC., Reeder, BJ., Jabeen, A., MacRobert, AJ., Ren, G. and Liang, X., (2016). Design and synthesis of 5-aminolaevulinic acid/3-hydroxypyridinone conjugates for photodynamic therapy: enhancement of protoporphyrin IX production and photo-toxicity in tumor cells. MedChemComm. 7 (6), 1190-1196

Zhu, C-F., Battah, S., Kong, X., Reeder, BJ., Hider, RC. and Zhou, T., (2015). Design, synthesis and biological evaluation of 5-aminolaevulinic acid/3-hydroxypyridinone conjugates as potential photodynamic therapeutical agents. Bioorganic & Medicinal Chemistry Letters. 25 (3), 558-561

Beckerson, P., Reeder, BJ. and Wilson, MT., (2015). Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding. FEBS Letters. 589 (4), 507-512

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

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

Reeder, BJ. and Hough, MA., (2014). The structure of a class 3 nonsymbiotic plant haemoglobin fromArabidopsis thalianareveals a novel N-terminal helical extension. Acta Crystallographica Section D Biological Crystallography. 70 (5), 1411-1418

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

Ascenzi, P., Marino, M., Polticelli, F., Coletta, M., Gioia, M., Marini, S., Pesce, A., Nardini, M., Bolognesi, M., Reeder, BJ. and Wilson, MT., (2013). Non-covalent and covalent modifications modulate the reactivity of monomeric mammalian globins. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1834 (9), 1750-1756

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

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

Reeder, BJ., (2010). The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms. Antioxidants & Redox Signaling. 13 (7), 1087-1123

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

Boutaud, O., Moore, KP., Reeder, BJ., Harry, D., Howie, AJ., Wang, S., Carney, CK., Masterson, TS., Amin, T., Wright, DW., Wilson, MT., Oates, JA. and Roberts, LJ., (2010). Acetaminophen inhibits hemoprotein-catalyzed lipid peroxidation and attenuates rhabdomyolysis-induced renal failure. Proceedings of the National Academy of Sciences. 107 (6), 2699-2704

Gaucher-Di Stasio, C., Paternotte, E., Prin-Mathieu, C., Reeder, BJ., Poitevin, G., Labrude, P., Stoltz, J-F., Cooper, CE. and Menu, P., (2009). The importance of the effect of shear stress on endothelial cells in determining the performance of hemoglobin based oxygen carriers. Biomaterials. 30 (4), 445-451

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

Reeder, BJ., Cutruzzola, F., Bigotti, MG., Hider, RC. and Wilson, MT., (2008). Tyrosine as a redox-active center in electron transfer to ferryl heme in globins. Free Radical Biology and Medicine. 44 (3), 274-283

Wilson, MT. and Reeder, BJ., (2008). Oxygen‐binding haem proteins. Experimental Physiology. 93 (1), 128-132

Reeder, BJ., Hider, RC. and Wilson, MT., (2008). Iron chelators can protect against oxidative stress through ferryl heme reduction. Free Radical Biology and Medicine. 44 (3), 264-273

Silaghi-Dumitrescu, R., Reeder, BJ., Nicholls, P., Cooper, CE. and Wilson, MT., (2007). Ferryl haem protonation gates peroxidatic reactivity in globins. Biochemical Journal. 403 (3), 391-395

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

Reeder, BJ., Cutruzzolà, F., Bigotti, MG., Watmough, NJ. and Wilson, MT., (2007). Histidine and not tyrosine is required for the Peroxide‐induced formation of haem to protein cross‐linked myoglobin. IUBMB Life. 59 (8-9), 477-489

Flors, C., (2006). Imaging the production of singlet oxygen in vivo using a new fluorescent sensor, Singlet Oxygen Sensor Green(R). Journal of Experimental Botany. 57 (8), 1725-1734

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

Vollaard, NBJ., Reeder, BJ., Shearman, JP., Menu, P., Wilson, MT. and Cooper, CE., (2005). A new sensitive assay reveals that hemoglobin is oxidatively modified in vivo. Free Radical Biology and Medicine. 39 (9), 1216-1228

Reeder, BJ. and Wilson, MT., (2005). Hemoglobin and Myoglobin Associated Oxidative Stress: from Molecular Mechanisms to Disease States. Current Medicinal Chemistry. 12 (23), 2741-2751

Reeder, BJ. and Wilson, MT., (2005). Desferrioxamine Inhibits Production of Cytotoxic Heme to Protein Cross-Linked Myoglobin:  A Mechanism to Protect against Oxidative Stress without Iron Chelation. Chemical Research in Toxicology. 18 (6), 1004-1011

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

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

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

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., Sharpe, MA., Kay, AD., Kerr, M., Moore, K. and Wilson, MT., (2002). Toxicity of myoglobin and haemoglobin: oxidative stress in patients with rhabdomyolysis and subarachnoid haemorrhage. Biochemical Society Transactions. 30 (4), 745-748

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

Reeder, BJ. and Wilson, MT., (2001). The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: a role for the protonated ferryl species. Free Radical Biology and Medicine. 30 (11), 1311-1318

Mason, MG., Ball, AS., Reeder, BJ., Silkstone, G., Nicholls, P. and Wilson, MT., (2001). Extracellular Heme Peroxidases in Actinomycetes: a Case of Mistaken Identity. Applied and Environmental Microbiology. 67 (10), 4512-4519

Holt, S., Reeder, B., Wilson, M., Harvey, S., Morrow, JD., Roberts, LJ. and Moore, K., (1999). Increased lipid peroxidation in patients with rhabdomyolysis. The Lancet. 353 (9160), 1241-1241

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

REEDER, JB. and WILSON, TM., (1998). Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoic acid. Biochemical Journal. 330 (3), 1317-1323

Rogers, MS., Patel, RP., Reeder, BJ., Sarti, P., Wilson, MT. and Alayash, AI., (1995). Pro-oxidant effects of cross-linked haemoglobins explored using liposome and cytochrome c oxidase vesicle model membranes. Biochemical Journal. 310 (3), 827-833

Reeder, B., Cutruzzola, F., Bigotti, M. and Wilson, M., (2004). An electron pathway through tyrosine facilitates reduction of pro-oxidant ferryl myoglobin by reducing agents.

Vollaard, N., Reeder, B., Shearman, J., Wilson, M. and Cooper, C., (2004). A new general method that reveals heme-protein mediated oxidative stress occurs in vivo and is increased during exercise

Reeder, BJ., Wilson, MT., Holt, S. and Moore, K., (1999). Haem to globin cross-linking is an in vivo marker for ferryl myoglobin induced oxidative stress