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Contact Details

Phone
+64 3 364 0898
Email
alexander.peskin@otago.ac.nz
Position
Research Fellow
Department
Department of Pathology and Biomedical Science (Christchurch)
Qualifications
DrSc PhD
Research summary
Antioxidants

Research

Dr Alexander Peskin graduated from Moscow State University and received his PhD and DSc (Habilitation) from the Russian Academy of Sciences. He worked as an Eleanor Roosevelt Fellow of the International Union Against Cancer at the Swiss Institute for Cancer Research (Cerutti lab) and as a Visiting Scientist at Lodz University (Bartosz lab), before joining the Centre for Free Radical Research in 1998.

Dr Peskin’s expertise lies in biochemistry and enzymology, with a particular interest in thiol biochemistry. His original research focussed on superoxide dismutase and cancer, and the biochemistry of chloramines, and more recently he has been investigating the complex biochemical properties of the peroxiredoxins.

Publications

Peskin, A. V. (2023). Could CO2 be a player in a redox relay team? Redox Biochemistry & Chemistry, 5-6, 100006. doi: 10.1016/j.rbc.2023.100006

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

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

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

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

Vissers, M. C. M., Pullar, J. M., & Peskin, A. V. (2018). Myeloperoxidase-derived oxidants hypochlorous acid and chloramines: Microbicidal marvels and inflammatory mischief makers. In M. C. M. Vissers, M. B. Hampton & A. J. Kettle (Eds.), Hydrogen peroxide metabolism in health and disease. (pp. 305-326). Boca Raton, FL: CRC Press.

Chapter in Book - Research

Peskin, A. V. (2023). Could CO2 be a player in a redox relay team? Redox Biochemistry & Chemistry, 5-6, 100006. doi: 10.1016/j.rbc.2023.100006

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

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

Kouakou Ahuie, G., Gagnon, H., Pace, P. E., Peskin, A. V., Wagner, P. R. J., Naylor, S., & Klarskov, K. (2020). Investigating protein thiol chemistry associated with dehydroascorbate, homocysteine and glutathione using mass spectrometry. Rapid Communications in Mass Spectrometry, 34, e8774. doi: 10.1002/rcm.8774

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

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

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

Yewdall, N. A., Peskin, A. V., Hampton, M. B., Goldstone, D. C., Pearce, F. G., & Gerrard, J. A. (2018). Quaternary structure influences the peroxidase activity of peroxiredoxin 3. Biochemical & Biophysical Research Communications, 497(2), 558-563. doi: 10.1016/j.bbrc.2018.02.093

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

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., & 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

Cheah, F.-C., Peskin, A. V., Wong, F.-L., Ithnin, A., Othman, A., & Winterbourn, C. C. (2014). Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants. FASEB Journal, 28(7), 3205-3210. doi: 10.1096/fj.14-250050

Journal - Research Article

Soethoudt, M., Peskin, A. V., Dickerhof, N., Paton, L. N., Pace, P. E., & Winterbourn, C. C. (2014). Interaction of adenanthin with glutathione and thiol enzymes: Selectivity for thioredoxin reductase and inhibition of peroxiredoxin recycling. Free Radical Biology & Medicine, 77, 331-339. doi: 10.1016/j.freeradbiomed.2014.09.025

Journal - Research Article

Pace, P. E., Peskin, A. V., Han, M.-H., Hampton, M. B., & Winterbourn, C. C. (2013). Hyperoxidized peroxiredoxin 2 interacts with the protein disulphide isomerase ERp46. Biochemical Journal, 453, 475-485. doi: 10.1042/BJ20130030

Journal - Research Article

Peskin, A. V., Dickerhof, N., Poynton, R. A., Paton, L. N., Pace, P. E., Hampton, M. B., & Winterbourn, C. C. (2013). Hyperoxidation of peroxiredoxins 2 and 3: Rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine. Journal of Biological Chemistry, 288, 14170-14177. doi: 10.1074/jbc.M113.460881

Journal - Research Article

Kato, Y., Peskin, A. V., Dickerhof, N., Harwood, D. T., & Kettle, A. J. (2012). Myeloperoxidase catalyzes the conjugation of serotonin to thiols via free radicals and tryptamine-4,5-dione. Chemical Research in Toxicology, 25(11), 2322-2332. doi: 10.1021/tx300218f

Journal - Research Article

Kelso, G. F., Maroz, A., Cochemé, H. M., Logan, A., Prime, T. A., Peskin, A. V., Winterbourn, C. C., James, A. M., … Brooker, S., Porteous, C. M., … Smith, R. A. J. (2012). A mitochondria-targeted macrocyclic Mn(II) superoxide dismutase mimetic. Chemistry & Biology, 19(10), 1237-1246. doi: 10.1016/j.chembiol.2012.08.005

Journal - Research Article

Karton, A., Nagy, P., Betz, A., Peskin, A. V., Pace, P., O'Reilly, R. J., Hampton, M. B., … Winterbourn, C. C. (2011). Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide; a kinetic and computational study. Journal of Biological Chemistry, 286(20), 18048-18055. doi: 10.1074/jbc.M111.232355

Journal - Research Article

Peskin, A. V., Cox, A. G., Nagy, P., Morgan, P. E., Hampton, M. B., Davies, M. J., & Winterbourn, C. C. (2010). Removal of amino acid, peptide and protein hydroperoxides by reaction with peroxiredoxins 2 and 3. Biochemical Journal, 432, 313-321. doi: 10.1042/BJ20101156

Journal - Research Article

Cox, A. G., Peskin, A. V., Paton, L. N., Winterbourn, C. C., & Hampton, M. B. (2009). Redox potential and peroxide reactivity of human peroxiredoxin 3. Biochemistry, 48(27), 6495-6501. doi: 10.1021/bi900558g

Journal - Research Article

Peskin, A. V., Turner, R., Maghzal, G. J., Winterbourn, C. C., & Kettle, A. J. (2009). Oxidation of methionine to dehydromethionine by reactive halogen species generated by neutrophils. Biochemistry, 48(42), 10175-10182. doi: 10.1021/bi901266w

Journal - Research Article

Stacey, M. M., Peskin, A. V., Vissers, M. C., & Winterbourn, C. C. (2009). Chloramines and hypochlorous acid oxidize erythrocyte peroxiredoxin 2. Free Radical Biology & Medicine, 47(10), 1468-1476. doi: 10.1016/j.freeradbiomed.2009.08.022

Journal - Research Article

Low, F. M., Hampton, M. B., Peskin, A. V., & Winterbourn, C. C. (2007). Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte. Blood, 109(6), 2611-2617.

Journal - Research Article

Peskin, A. V., Low, F. M., Paton, L. N., Maghzal, G. J., Hampton, M. B., & Winterbourn, C. C. (2007). The high reactivity of peroxiredoxin 2 with H2O2 is not reflected in its reaction with other oxidants and thiol reagents. Journal of Biological Chemistry, 282(16), 11885-11892.

Journal - Research Article

Peskin, A. V., & Winterbourn, C. C. (2006). Taurine chloramine is more selective than hypochlorous acid at targeting critical cysteines and inactivating creatine kinase and glyceraldehyde-3-phosphate dehydrogenase. Free Radical Biology & Medicine, 40, 45-53.

Journal - Research Article

Peskin, A. V., Midwinter, R. G., Harwood, D. T., & Winterbourn, C. C. (2005). Chlorine transfer between glycine, taurine, and histamine: Reaction rates and impact on cellular reactivity [Erratum version of the 2004 publication of the same title]. Free Radical Biology & Medicine, 38(3), 397-405.

Journal - Research Article

Midwinter, R. G., Peskin, A. V., Vissers, M. C. M., & Winterbourn, C. C. (2004). Extracellular oxidation by taurine chloramine activates ERK via the epidermal growth factor receptor. Journal of Biological Chemistry, 279(31), 32205-32211.

Journal - Research Article

Peskin, A. V., & Winterbourn, C. C. (2003). Histamine chloramine reactivity with thiol compounds, ascorbate, and methionine and with intracellular glutathione. Free Radical Biology & Medicine, 35(10), 1252-1260.

Journal - Research Article

Winterbourn, C. C., Peskin, A. V., & Parsons-Mair, H. N. (2002). Thiol oxidase activity of copper, zinc superoxide dismutase. Journal of Biological Chemistry, 277(3), 1906-1911.

Journal - Research Article

Wood, J. E., Senthilmohan, S. T., & Peskin, A. (2002). Antioxidant activity of procyanidin-containing plant extracts at different pHs. Food Chemistry, 77(2), 155-161.

Journal - Research Article

Peskin, A. V., & Winterbourn, C. C. (2001). Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate. Free Radical Biology & Medicine, 30, 572-579.

Journal - Research Article

Peskin, A., & Winterbourn, C. C. (2000). A microtiter plate assay for superoxide dismutase using a water soluble tetrazolium salt (WST-1). Clinica Chimica Acta, 293, 157-166.

Journal - Research Article

Peskin, A. (2003). Science and political dictatorship [Correspondence]. Nature Reviews Genetics. Retrieved from http://www.nature.com/nrg/archive/correspondence_mf.html

Journal - Research Other

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