People

Dr Brandon Reeder

Senior Lecturer
School of Life Sciences
Dr Brandon Reeder
  • Email

  • Telephone

    +44 (0) 1206 872119

  • Location

    3SW.6.15, Colchester Campus

  • Academic support hours

    9am to 5 pm, Monday to Friday

Profile

Biography

Senior Lecturer in Biochemistry and Molecular Biophysics Twitter: @BrandonJReeder1 Lab no: 6.19 Lab ext: 3015 Senior Fellow of the Higher Education Academy Society membership: Biochemical Society (since 1994) British Biophysical Society ORCID ID: http://orcid.org/0000-0001-7474-2611 Google Scholar citations: http://scholar.google.co.uk/citations?user=10SbOKkAAAAJ&hl=en Current publication h-index:31 Citations: >4000 Positions open for high-quality self-funded students to do PhD or MSc (research)in my laboratory. Applications or informal inquiries welcome. Current Group Members: Dr Elizabeth Welbourn (p/t): Technician Dr Sinan Battah: Vistiting Scientist Miss Hana Abarra (p/t): PhD student Mr Jeffrey Asaju: PhD student Former Group Members Dr Michelle Simons: Postdoctoral researcher - funded by MRC Dr Victoria Allen-Baume(p/t) - Research Technician funded by BBSRC/MRC Dr Nelida Leiva Eriksson: Postdoctoral researcher - funded by MRC Dr Badri Rajagopal: Postdoctoral researcher - funded by the BBSRC Dr Svetlana Gretton: Postdoctoral researcher - funded by MRC Mrs Thoufieq Shaik: Research Technician- funded by the BBSRC Dr Gary Silkstone: Postdoctoral researcher - funded by the BBSRC/MRC Dr Natalie Syrett- Research Technician funded by MRC Miss Julie Double(p/t): Technician Mr (Dr) John Ukeri: PhD Student. Miss (Dr) Penny Beckerson: PhD student Mrs Georgia Scobioala: MSD student, Christine Desty Scholarship Miss Sareeta Bagri: MSD student, Christine Desty Scholarship Career history: 2020-Present Senior Lecturer (Associate Professor) of Biochemistry and Molecular Biophysics, Department of Biological Sciences, University of Essex, UK 2011-2020 Lecturer (Assistant Professor) 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-center 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.

Qualifications

  • PhD. Biological Chemistry University of Essex, (1998)

  • MSc. Biological Chemistry University of Essex, (1994)

  • BSc. Biological and Medicinal Chemistry University of Essex, (1993)

Appointments

University of Essex

  • Senior Lecturer in Biochemistry and Molceular Biophysics, Life Sciences, University of Essex (16/12/2020 - present)

  • Lecturer in Biochemistry and Molceular Biophysics, Biological Sciences, University of Essex (1/1/2011 - 16/12/2020)

  • Senior Research Officer, Biological Sciences, University of Essex (1/2/2008 - 31/12/2010)

  • Senior Research Officer, Biological Sciences, University of Essex (1/1/2006 - 31/12/2007)

Research and professional activities

Research interests

Biochemical and Biomedical based-research, particularly in the role of proteins in health and disease.

Open to supervise

Metalloproteins in health and disease:

Open to supervise

The next generation of blood substitutes

Key words: blood
Open to supervise

Role of human cytoglobin in lipid binding, lipid oxidation, cell signalling and cancer therapy resistance.

Open to supervise

Role of neuroglobin in cell signalling and cell protection in neurodegenerative diseases such as Alzheimers.

Open to supervise

Biochemical mechanisms oxidative stress in acute renal failure following rhabdomyolysis and delayed vasospasm following subarachnoid haemorrhage.

Open to supervise

Cell signalling by oxidatively modified lipids and formation of singlet oxygen resulting from lipid oxidation.

Open to supervise

Developing novel compounds as ameliorators of haemoprotein-induced oxidative reactions.

Open to supervise

Current research

Molecular function of Androglobin on ciliogenesis

Androglobin is a newly discovered protein that has some highly unusual features. We are the first lab to be able to generate domains of the protein recombinantly. We are exploring how the molecular structure and function of this protein is involved in ciliogenesis, the formation of cilia in human cells.

Next generation of Artificial oxygen carriers for oxygen therapeutics and blood substitutes.

Artificial, cell free Hemoglobin-based oxygen carriers are an ideal blood substitute – in theory. After 40 years of research there are still issues with this potential life saving technology. At Essex we have developed a new generation of genetically engineered artificial Hemoglobin-based oxygen carriers for use in treatment of specific conditions including trauma and Sickle Cell crisis.
More information about this project

Conferences and presentations

A multi-targeted approach to engineer a safer generation of hemoglobin-based oxygen carrier

Invited presentation, International Society on Oxygen Transport to Tissue, Monte Verità Conferencre Center, Ascona, Switzerland, 22/9/2022

Expression and characterization of a stable form of the circularly permuted globin domain of human androglobin

Invited presentation, • XXI International Conference on Oxygen Binding and Sensing Proteins, Roma, Italy, 7/9/2022

Teaching and supervision

Current teaching responsibilities

  • Haematology and Blood Transfusion Science (BS236)

  • Structural and Molecular Enzymology (BS314)

  • Research Project in Biomedical Science (BS831)

  • Research Project in Life Sciences (BS832)

Previous supervision

Sareeta Bagri
Sareeta Bagri
Thesis title: Molecular Assembly and Function of Androglobin, a Novel Chimeric Globin.
Degree subject: Biochemistry
Degree type: Master of Science (by Dissertation)
Awarded date: 17/5/2021
Georgia Louise Scobioala
Georgia Louise Scobioala
Thesis title: Exploring the Molecular Mechanisms of Human Cytoglobin and its Role in Cancer
Degree subject: Molecular Medicine
Degree type: Master of Science (by Dissertation)
Awarded date: 8/4/2021
John Junior Ukeri
John Junior Ukeri
Thesis title: Studies of the Effect of Cysteine and Heme Pocket Mutations of the Nitric Oxide Dioxygenase and Nitrite Reductase Activities of Human Cytoglobin and Androglobin Heme Domain
Degree subject: Cell and Molecular Biology
Degree type: Doctor of Philosophy
Awarded date: 24/8/2020
Penny Beckerson
Penny Beckerson
Thesis title: Studies of the Effect of Cysteine Modifications, Distal Haem Pocket Mutations and Lipid Interaction on the Reactions of Cytoglobin
Degree subject: Biochemistry
Degree type: Doctor of Philosophy
Awarded date: 29/6/2015

Publications

Publications (1)

Exposito-Rodriguez, M., Reeder, B., Brooke, GN., Hough, MA., Laissue, PP. and Mullineaux, PM., (2024). A novel glutathione peroxidase-based biosensor disentangles differential subcellular accumulation of H2O2 and lipid hydroperoxides

Journal articles (61)

Reeder, BJ., (2023). Globin Associated Oxidative Stress. Antioxidants. 12 (5), 1077-1077

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

Books (1)

Cooper, CE., Bird, M., Sheng, X., Simons, M., Ronda, L., Mozzarelli, A. and Reeder, BJ., (2022). Stability of a Novel PEGylation Site on a Putative Haemoglobin-Based Oxygen Carrier. Springer International Publishing. 9783031141898

Book chapters (3)

Silkstone, GGA., Simons, M., Rajagopal, BS., Shaik, T., Reeder, BJ. and Cooper, CE., (2018). Novel Redox Active Tyrosine Mutations Enhance the Regeneration of Functional Oxyhemoglobin from Methemoglobin: Implications for Design of Blood Substitutes.. In: Oxygen Transport to Tissue XL. Editors: Thews, O., LaManna, J. and Harrison, D., . Springer. 221- 225. 978-3-319-91285-1

Wilson, MT. and Reeder, BJ., (2006). MYOGLOBIN. In: Encyclopedia of Respiratory Medicine. Elsevier. 73- 76. 9780123708793

Wilson, MT. and Reeder, BJ., (2006). MYOGLOBIN. In: Encyclopedia of Respiratory Medicine: Volume 1-4. V3-73-V3-76. 9780123708793

Conferences (7)

Thompson, MK., Franzen, S., Ghiladi, RA., Reeder, BJ. and Svistunenko, DA., (2011). Decay of Compound ES in Dehaloperoxidase-Hemoglobin

Reeder, BJ., Svistunenko, DA., Cooper, CE. and Wilson, MT., (2009). Engineering Electron Transfer Pathways in Myoglobin and Hemoglobin: A Route to Detoxify Blood Substitutes?

Reeder, BJ., Nilson, M., Bulow, L., Cooper, CE. and Wilson, MT., (2007). Modulating electron transfer pathways in hemoglobin

Boutaud, O., Wang, SH., Amin, T., Moore, K., Wilson, M., Reeder, BJ., Roberts, LJ. and Oates, J., (2006). Inhibition by acetaminophen of ferryl-hemoprotein-induced oxidation of arachidonic acid

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

Reports and Papers (1)

Reeder, B., Deganutti, G., Ukeri, J., Atanasio, S., Svistunenko, D., Ronchetti, C., Mobarec, JC., Welbourn, E., Asaju, J., Vos, M., Wilson, M. and Reynolds, C., (2024). The circularly permuted globin domain of Androglobin exhibits atypical heme stabilization and nitric oxide interaction

Grants and funding

2020

Replacement EPR spectrometer to the multiuser Biomedical EPR Facility at the University of Essex

Biotechnology and Biological Sciences Research Council

Optimisation of the manufacture of a homogeneous synthetic haemoglobin as a novel Oxygen Therapeutic / Blood Substitute

Medical Research Council

2019

Protein Detection Kit

East Suffolk and North Essex NHS Foundation Trust

2013

The Effect of Iron levels on the Magnesium Isotope Effects on Creatine Kinase Activity

Emf Biological Research Trust

Engineering a new generation of blood substitutes

Medical Research Council

Creating an Effective and Non Toxic Blood Substitute

Biotechnology & Biology Science Res.Council

2012

THe Role of Non-Symbiotic Plant Haemoglobin structure & fundction in cell Signalling

The Royal Society

Creating an effective and non toxic blood substitute

Biotechnology & Biology Science Res.Council

Contact

reedb@essex.ac.uk
+44 (0) 1206 872119

Location:

3SW.6.15, Colchester Campus

Academic support hours:

9am to 5 pm, Monday to Friday

More about me
Blood Substitutes Webpage: http://www.haemo2.com/

Follow me on social media