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Alexander PeskinResearch Fellow

BSc, DrSc, PhD(Moscow)

Email alexander.peskin@otago.ac.nz
Tel +64 3 364 0898

Research interests

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.

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Publications

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

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

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

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.

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., & 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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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Journal - Research Other

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

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Conference Contribution - Published proceedings: Abstract

Pace, P., Peskin, A. V., Jasoni, C. L., Winterbourn, C., & Hampton, M. (2016). Interaction of peroxiredoxin 2 with collapsin response mediator protein 2. Free Radical Biology & Medicine, 100(Suppl.), (pp. S47). doi: 10.1016/j.freeradbiomed.2016.10.126

Peskin, A., Pace, P., Behring, J., Paton, L., Soethoudt, M., Bachschmid, M., & Winterbourn, C. (2015). Glutathionylation at the Active Sites of Peroxiredoxin 2 and Recycling by Glutaredoxin. Free Radical Biology & Medicine, 87(Suppl. 1), (pp. 105). doi: 10.1016/j.freeradbiomed.2015.10.276

Winterbourn, C. C., Cheah, F.-C., & Peskin, A. V. (2014). Increased basal oxidation and limited recycling of peroxiredoxin 2 in glucose-6-phosphate dehydrogenase deficient erythrocytes. Free Radical Biology & Medicine, 76(Suppl. 1), (pp. S161). doi: 10.1016/j.freeradbiomed.2014.10.075

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Conference Contribution - Poster Presentation (not in published proceedings)

Pace, P. E., Peskin, A. V., Han, M.-H., Hampton, M. B., & Winterbourn, C. C. (2013, August). Hyperoxidized peroxiredoxin 2 interacts with the protein disulphide isomerase ERp46. Poster session presented at the Queenstown Molecular Biology (QMB) Meetings, Queenstown, New Zealand.

Peskin, A. V., Dickerhof, N., Paton, L. N., Poynton, R. A., Pace, P., Hampton, M. B., & Winterbourn, C. C. (2013, August). Hyperoxidation of human peroxiredoxin 2 and 3. Poster session presented at the Queenstown Molecular Biology (QMB) Meetings, Queenstown, New Zealand.

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Conference Contribution - Verbal presentation and other Conference outputs

Peskin, A. (2014, July). Increased basal oxidation of preoxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants. Verbal presentation at the Oxygen Theme Meeting, Christchurch, New Zealand.

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