Principal Investigator
MSc (Auckland), PhD (Massey) CNZM, FRSNZ
Education
Professor Christine Winterbourn is an Auckland University chemistry graduate who received her PhD in biochemistry from Massey University.
She did postdoctoral work at the University of British Columbia, Canada before returning to the Pathology Department, University of Otago, Christchurch, where she now has a personal chair.
Research interests
Professor Winterbourn has published more than 250 scientific papers. Her field of research is the biological chemistry of free radicals and other reactive oxidants and their involvement in health and disease.
Professor Winterbourn's focus is on understanding mechanisms of reactive oxidant production, the biochemistry of biological damage and the consequences for disease pathology.
Her current interests include:
- the production of reactive oxidants by neutrophils and their involvement in microbial killing and inflammation
- how neutrophils form extracellular traps (NETs)
- how thiol proteins contribute to antioxidant defence and redox regulated cell signaling
- biochemistry and cellular functions of mammalian peroxiredoxins
- mechanisms of oxidative protein crosslinking
- oxidant-antioxidant interactions in red blood cells
Other positions
- Past member of the Health Research Council
- Past member of the Marsden Fund Council
- Editor of the Biochemical Journal
- Editorial Board of Free Radical Biology and Medicine
Awards
- University of Auckland Distinguished Alumni 2015
- Royal Society of New Zealand’s Rutherford Medal - the first woman to receive the award in its 20 year history
- NZ Association of Scientists’ Marsden Medal
- Massey University 75th Anniversary Medal
- Society for Free Radical Research (Australasia) Distinguished Service Award
- University of Otago Distinguished Research Medal and Society for Free Radical Research (International) Trevor Slater Award
Publications
Winterbourn, C. C., Peskin, A., Kleffmann, T., Radi, R., & Pace, P. E. (2023). Carbon dioxide/bicarbonate is required for sensitive inactivation of mammalian glyceraldehyde-3-phosphate dehydrogenase by hydrogen peroxide. PNAS, 120(18), e2221047120. doi: 10.1073/pnas.2221047120
Magon, N. J., Turner, R., Kettle, A. J., & Winterbourn, C. C. (2023). Cross-linking between cysteine and lysine, tryptophan or tyrosine in peptides and proteins treated with hypochlorous acid and other reactive halogens. Redox Biochemistry & Chemistry. Advance online publication. doi: 10.1016/j.rbc.2023.100002
Kettle, A. J., Ashby, L. V., Winterbourn, C. C., & Dickerhof, N. (2023). Superoxide: The enigmatic chemical chameleon in neutrophil biology [Invited review]. Immunological Reviews. Advance online publication. doi: 10.1111/imr.13183
Pace, P. E., Peskin, A. V., Winterbourn, C. C., & Hampton, M. B. (2022, August). Disrupting the oligomeric structure of peroxiredoxins in cancer cells using CRISPR. Poster session presented at the CRISPR Technologies Satellite Meeting: Queenstown Research Week, Queenstown, New Zealand.
Pace, P., & Winterbourn, C. C. (2022). A cautionary note on using phosphatase inhibitors with hydrogen peroxide. Antioxidants & Redox Signaling. Advance online publication. doi: 10.1089/ars.2022.0092
Winterbourn, C. C. (2019). Reactive oxygen species in biological systems. In E. Niki (Ed.), Food chemistry, function and analysis. (pp. 98-117). London, UK: Royal Society of Chemistry. doi: 10.1039/9781788016216-00098
Chapter in Book - Research
Kettle, A. J., & Winterbourn, C. C. (2016). Myeloperoxidase: Structure and function of the green heme peroxidase of neutrophils. In E. Raven & B. Dunford (Eds.), Heme peroxidases. (pp. 272-308). Cambridge, UK: Royal Society of Chemistry. doi: 10.1039/9781782622628-00272
Chapter in Book - Research
Parker, H. A., Magon, N. J., Green, J. N., Hampton, M. B., & Winterbourn, C. C. (2014). Analysis of neutrophil bactericidal activity. In M. T. Quinn & F. R. DeLeo (Eds.), Neutrophil methods and protocols: Methods in Molecular Biology (Vol. 1124). (2nd ed.) (pp. 291-306). New York, NY: Springer. doi: 10.1007/978-1-62703-845-4_19
Chapter in Book - Research
Winterbourn, C. C. (2013). The biological chemistry of hydrogen peroxide. In E. Cadenas & L. Packer (Eds.), Methods in enzymology: Hydrogen peroxide and cell signaling: Part C (Vol. 528). (pp. 3-25). Waltham, MA: Academic Press. doi: 10.1016/B978-0-12-405881-1.00001-X
Chapter in Book - Research
Winterbourn, C. C. (2012). Biological chemistry of reactive oxygen species. In C. Chatgilialoglu & A. Studer (Eds.), Encyclopedia of radicals in chemistry, biology and materials. (pp. 1259-1281). Chichester, UK: Wiley. doi: 10.1002/9781119953678.rad077
Chapter in Book - Research
Cox, A. G., Winterbourn, C. C., & Hampton, M. B. (2010). Measuring the redox state of cellular peroxiredoxins by immunoblotting. In E. Cadenas & L. Packer (Eds.), Methods in enzymology: Thiol redox transitions in cell signaling: Part B: Cellular localization and signaling (Vol. 474). (pp. 51-66). San Diego, CA: Academic Press. doi: 10.1016/S0076-6879(10)74004-0
Chapter in Book - Research
Nagy, P., & Winterbourn, C. C. (2010). Redox chemistry of biological thiols. In J. C. Fishbein (Ed.), Advances in molecular toxicology (Vol. 4). (pp. 223-266). Amsterdam, The Netherlands: Elsevier.
Chapter in Book - Research
Green, J. N., Winterbourn, C. C., & Hampton, M. B. (2007). Analysis of neutrophil bactericidal activity. In M. T. Quinn, F. R. DeLeo & G. M. Bokoch (Eds.), Neutrophil methods and protocols. (pp. 319-332). Totowa, USA: Humana Press.
Chapter in Book - Research
Hampton, M. B., Baty, J. W., & Winterbourn, C. C. (2006). Use of a proteomic technique to identify oxidant-sensitive thiol proteins in cultured cells. In I. Dalle-Donne, A. Scaloni & D. A. Butterfield (Eds.), Redox Proteomics: From protein modifications to cellular dysfunction and diseases. (pp. 253-265). Hoboken, NJ: John Wiley & Sons.
Chapter in Book - Research
Winterbourn, C. C. (2003). Radical scavenging by thiols: Biological significance and implications for redox signaling and antioxidant defense. In C. Gitler & A. Danon (Eds.), Cellular implications of redox signaling. (pp. 175-190). London: Imperial College Press.
Chapter in Book - Research
Buss, I. H., Winterbourn, C. C., & Armstrong, D. A. (2002). Protein carbonyl measurement by ELISA. In Free Radicals and Antioxidants Protocols, Volume 186, Totowa. (pp. 123-128). Gainsville, Florida: The Humana Press Inc.
Chapter in Book - Research
Winterbourn, C. C., van Dalen, C. J., Hampton, M. B., & Kettle, A. J. (2000). Reactions of myeloperoxidase and production of hypochlorous acid in neutrophil phagosomes. In P. E. Petrides & W. M. Nauseef (Eds.), The Peroxidase Multigene Family of Enzymes. (pp. 58-67). Berlin: Springer.
Chapter in Book - Research
McPherson, K. G., Kettle, A. J., & Winterbourn, C. C. (1997). Mechanism of activation of NFKB by hydrogen peroxide in Jurkat JR cells. In L. Montagnier, R. Olivier & C. Pasquier (Eds.), Oxidative Stress and Redox Regulation: Cellular Signalling, Aids, Cancer and Other Diseases. (pp. 83-87). New York: Marcel Dekker.
Chapter in Book - Research
Kettle, A. J., & Winterbourn, C. C. (1996). Reaction mechanisms of myeloperoxidase. In C. Obinger, U. Burner, R. Ebermann, C. Penel & H. Greppin (Eds.), Plant Peroxidases: Biochemistry and Physiology. (pp. 134-139). Geneva: University of Geneva.
Chapter in Book - Research
Winterbourn, C. C. (1996). Free radicals, oxidants and antioxidants. In R. D. G. Milner (Ed.), Perinatal and Pediatric Pathophysiology: A Clinical Perspective. 2nd edn. (pp. 108-115). London: Edward Arnold.
Chapter in Book - Research
Winterbourn, C., & Kettle, T. (2013). Centre for Free Radical Research. In P. Joyce, G. Nicholls, K. Thomas & T. Wilkinson (Eds.), The Christchurch experience: 40 years of research and teaching. (pp. 75-78). Christchurch, New Zealand: University of Otago.
Chapter in Book - Other
Magon, N. J., Turner, R., Kettle, A. J., & Winterbourn, C. C. (2023). Cross-linking between cysteine and lysine, tryptophan or tyrosine in peptides and proteins treated with hypochlorous acid and other reactive halogens. Redox Biochemistry & Chemistry. Advance online publication. doi: 10.1016/j.rbc.2023.100002
Journal - Research Article
Winterbourn, C. C., Peskin, A., Kleffmann, T., Radi, R., & Pace, P. E. (2023). Carbon dioxide/bicarbonate is required for sensitive inactivation of mammalian glyceraldehyde-3-phosphate dehydrogenase by hydrogen peroxide. PNAS, 120(18), e2221047120. doi: 10.1073/pnas.2221047120
Journal - Research Article
Königstorfer, A., Ashby, L. V., Bollar, G. E., Billiot, C. E., Gray, M. J., Jakob, U., Hampton, M. B., & Winterbourn, C. C. (2021). Induction of the reactive chlorine-responsive transcription factor RclR in Escherichia coli following ingestion by neutrophils. Pathogens & Disease, 79, ftaa079. doi: 10.1093/femspd/ftaa079
Journal - Research Article
Parker, H. A., Jones, H. M., Kaldor, C. D., Hampton, M. B., & Winterbourn, C. C. (2021). Neutrophil NET formation with microbial stimuli requires late stage NADPH oxidase activity. Antioxidants, 10, 1791. doi: 10.3390/antiox10111791
Journal - Research Article
Paumann-Page, M., Kienzl, N. F., Motwani, J., Bathish, B., Paton, L. N., Magon, N. J., … Eccles, M. R., & Winterbourn, C. C. (2021). Peroxidasin protein expression and enzymatic activity in metastatic melanoma cell lines are associated with invasive potential. Redox Biology, 46, 102090. doi: 10.1016/j.redox.2021.102090
Journal - Research Article
Peskin, A. V., & Winterbourn, C. C. (2021). The enigma of 2-Cys peroxiredoxins: What are their roles? Biochemistry (Moscow), 86(1), 84-91. doi: 10.1134/S0006297921010089
Journal - Research Article
Peskin, A. V., Meotti, F. C., Kean, K. M., Göbl, C., Peixoto, A. S., Pace, P. E., … Winterbourn, C. C. (2021). Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2. Journal of Biological Chemistry, 296, 100494. doi: 10.1016/j.jbc.2021.100494
Journal - Research Article
Queiroz, R. F., Stanley, C. P., Wolhuter, K., Kong, S. M. Y., Rajivan, R., McKinnon, N., … Winterbourn, C. C., … Stocker, R. (2021). Hydrogen peroxide signaling via its transformation to a stereospecific alkyl hydroperoxide that escapes reductive inactivation. Nature Communications, 12, 6626. doi: 10.1038/s41467-021-26991-5
Journal - Research Article
Bathish, B., Paumann-Page, M., Paton, L. N., Kettle, A. J., & Winterbourn, C. C. (2020). Peroxidasin mediates bromination of tyrosine residues in the extracellular matrix. Journal of Biological Chemistry, 295(36), 12697-12705. doi: 10.1074/jbc.RA120.014504
Journal - Research Article
Mohammad, A., Saini, R. V., Kumar, R., Sharma, D., Saini, N. K., Gupta, A., … Winterbourn, C. C., & Saini, A. K. (2020). A curious case of cysteines in human peroxiredoxin I. Redox Biology, 37, 101738. doi: 10.1016/j.redox.2020.101738
Journal - Research Article
O'Connor, K. M., Das, A. B., Winterbourn, C. C., & Hampton, M. B. (2020). Inhibition of DNA methylation in proliferating human lymphoma cells by immune cell oxidants. Journal of Biological Chemistry, 295(23), 7839-7848. doi: 10.1074/jbc.RA120.013092
Journal - Research Article
Peskin, A. V., Meotti, F. C., de Souza, L. F., Anderson, R. F., Winterbourn, C. C., & Salvador, A. (2020). Intra-dimer cooperativity between the active site cysteines during the oxidation of peroxiredoxin 2. Free Radical Biology & Medicine, 158, 115-125. doi: 10.1016/j.freeradbiomed.2020.07.007
Journal - Research Article
Winterbourn, C. C. (2020). Biological chemistry of superoxide radicals. ChemTexts, 6, 7. doi: 10.1007/s40828-019-0101-8
Journal - Research Article
Dagnell, M., Cheng, Q., Rizvi, S. H. M., Pace, P. E., Boivin, B., Winterbourn, C. C., & Arnér, E. S. J. (2019). Bicarbonate is essential for protein-tyrosine phosphatase 1B (PTP1B) oxidation and cellular signaling through EGF-triggered phosphorylation cascades. Journal of Biological Chemistry, 294(33), 12330-12338. doi: 10.1074/jbc.RA119.009001
Journal - Research Article
de Souza, L. F., Pearson, A. G., Pace, P. E., Dafre, A. L., Hampton, M. B., Meotti, F. C., & Winterbourn, C. C. (2019). Peroxiredoxin expression and redox status in neutrophils and HL-60 cells. Free Radical Biology & Medicine, 135, 227-234. doi: 10.1016/j.freeradbiomed.2019.03.007
Journal - Research Article
Kumar, R., Mohammad, A., Saini, R. V., Chahal, A., Wong, C.-M., Sharma, D., … Winterbourn, C. C., & Saini, A. K. (2019). Deciphering the in vivo redox behavior of human peroxiredoxins I and II by expressing in budding yeast. Free Radical Biology & Medicine, 145, 321-329. doi: 10.1016/j.freeradbiomed.2019.09.034
Journal - Research Article
Peskin, A. V., Pace, P. E., & Winterbourn, C. C. (2019). Enhanced hyperoxidation of peroxiredoxin 2 and peroxiredoxin 3 in the presence of bicarbonate/CO2. Free Radical Biology & Medicine, 145, 1-7. doi: 10.1016/j.freeradbiomed.2019.09.010
Journal - Research Article
Albrett, A. M., Ashby, L. V., Dickerhof, N., Kettle, A. J., & Winterbourn, C. C. (2018). Heterogeneity of hypochlorous acid production in individual neutrophil phagosomes revealed by a rhodamine-based probe. Journal of Biological Chemistry, 293(40), 15715-15724. doi: 10.1074/jbc.RA118.004789
Journal - Research Article
Bathish, B., Turner, R., Paumann-Page, M., Kettle, A. J., & Winterbourn, C. C. (2018). Characterisation of peroxidasin activity in isolated extracellular matrix and direct detection of hypobromous acid formation. Archives of Biochemistry & Biophysics, 646, 120-127. doi: 10.1016/j.abb.2018.03.038
Journal - Research Article
Coker, M. S., Forbes, L. V., Plowman-Holmes, M., Murdoch, D. R., Winterbourn, C. C., & Kettle, A. J. (2018). Interactions of staphyloxanthin and enterobactin with myeloperoxidase and reactive chlorine species. Archives of Biochemistry & Biophysics, 646, 80-89. doi: 10.1016/j.abb.2018.03.039
Journal - Research Article
Das, A. B., Sadowska-Bartosz, I., Königstorfer, A., Kettle, A. J., & Winterbourn, C. C. (2018). Superoxide dismutase protects ribonucleotide reductase from inactivation in yeast. Free Radical Biology & Medicine, 116, 114-122. doi: 10.1016/j.freeradbiomed.2018.01.001
Journal - Research Article
Pace, P. E., Peskin, A. V., Konigstorfer, A., Jasoni, C. L., Winterbourn, C. C., & Hampton, M. B. (2018). Peroxiredoxin interaction with the cytoskeletal-regulatory protein CRMP2: Investigation of a putative redox relay. Free Radical Biology & Medicine, 129, 383-393. doi: 10.1016/j.freeradbiomed.2018.10.407
Journal - Research Article
Dagnell, M., Pace, P. E., Cheng, Q., Frijhoff, J., Östman, A., Arnér, E. S. J., Hampton, M. B., & Winterbourn, C. C. (2017). Thioredoxin reductase 1 and NADPH directly protect protein tyrosine phosphatase 1B from inactivation during H2O2 exposure. Journal of Biological Chemistry, 292(35), 14371-14380. doi: 10.1074/jbc.M117.793745
Journal - Research Article
Green, J. N., Chapman, A. L. P., Bishop, C. J., Winterbourn, C. C., & Kettle, A. J. (2017). Neutrophil granule proteins generate bactericidal ammonia chloramine on reaction with hydrogen peroxide. Free Radical Biology & Medicine, 113, 363-371. doi: 10.1016/j.freeradbiomed.2017.10.343
Journal - Research Article
Peskin, A. V., & Winterbourn, C. C. (2017). Assay of superoxide dismutase activity in a plate assay using WST-1. Free Radical Biology & Medicine, 103, 188-191. doi: 10.1016/j.freeradbiomed.2016.12.033
Journal - Research Article
Bayer, S. B., Low, F. M., Hampton, M. B., & Winterbourn, C. C. (2016). Interactions between peroxiredoxin 2, hemichrome and the erythrocyte membrane. Free Radical Research, 50(12), 1329-1339. doi: 10.1080/10715762.2016.1241995
Journal - Research Article
Bekeschus, S., Winterbourn, C. C., Kolata, J., Masur, K., Hasse, S., Bröker, B. M., & Parker, H. A. (2016). Neutrophil extracellular trap formation is elicited in response to cold physical plasma. Journal of Leukocyte Biology, 100(4), 791-799. doi: 10.1189/jlb.3A0415-165RR
Journal - Research Article
Peskin, A. V., Pace, P. E., Behring, J. B., Paton, L. N., Soethoudt, M., Bachschmid, M. M., & Winterbourn, C. C. (2016). Glutathionylation of the active site cysteines of peroxiredoxin 2 and recycling by glutaredoxin. Journal of Biological Chemistry, 291(6), 3053-3062. doi: 10.1074/jbc.M115.692798
Journal - Research Article
Poynton, R. A., Peskin, A. V., Haynes, A. C., Lowther, W. T., Hampton, M. B., & Winterbourn, C. C. (2016). Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidation. Biochemical Journal, 473, 411-421. doi: 10.1042/bj20150572
Journal - Research Article
Winterbourn, C. C. (2016). Revisiting the reactions of superoxide with glutathione and other thiols. Archives of Biochemistry & Biophysics, 595, 68-71. doi: 10.1016/j.abb.2015.11.028
Journal - Research Article
Winterbourn, C. C., & Peskin, A. V. (2016). Kinetic approaches to measuring peroxiredoxin reactivity. Molecules & Cells, 39(1), 26-30. doi: 10.14348/molcells.2016.2325
Journal - Research Article
Bayer, S. B., Hampton, M. B., & Winterbourn, C. C. (2015). Accumulation of oxidized peroxiredoxin 2 in red blood cells and its prevention. Transfusion, 55(8), 1909-1918. doi: 10.1111/trf.13039
Journal - Research Article
Wilkie-Grantham, R. P., Magon, N. J., Harwood, D. T., Kettle, A. J., Vissers, M. C., Winterbourn, C. C., & Hampton, M. B. (2015). Myeloperoxidase-dependent lipid peroxidation promotes the oxidative modification of cytosolic proteins in phagocytic neutrophils. Journal of Biological Chemistry, 290(15), 9896-9905. doi: 10.1074/jbc.M114.613422
Journal - Research Article
Bekeschus, S., Kolata, J., Winterbourn, C., Kramer, A., Turner, R., Weltmann, K. D., … Masur, K. (2014). Hydrogen peroxide: A central player in physical plasma-induced oxidative stress in human blood cells. Free Radical Research, 48(5), 542-549. doi: 10.3109/10715762.2014.892937
Journal - Research Article