JOURNAL BROWSE
Search
Advanced SearchSearch Tips
Kinetic Approaches to Measuring Peroxiredoxin Reactivity
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
  • Journal title : Molecules and Cells
  • Volume 39, Issue 1,  2016, pp.26-30
  • Publisher : Korea Society for Molecular and Cellular Biology
  • DOI : 10.14348/molcells.2016.2325
 Title & Authors
Kinetic Approaches to Measuring Peroxiredoxin Reactivity
Winterbourn, Christine C.; Peskin, Alexander V.;
  PDF(new window)
 Abstract
Peroxiredoxins are ubiquitous thiol proteins that catalyse the breakdown of peroxides and regulate redox activity in the cell. Kinetic analysis of their reactions is required in order to identify substrate preferences, to understand how molecular structure affects activity and to establish their physiological functions. Various approaches can be taken, including the measurement of rates of individual steps in the reaction pathway by stopped flow or competitive kinetics, classical enzymatic analysis and measurement of peroxidase activity. Each methodology has its strengths and they can often give complementary information. However, it is important to understand the experimental conditions of the assay so as to interpret correctly what parameter is being measured. This brief review discusses different kinetic approaches and the information that can be obtained from them.
 Keywords
hyperoxidation;kinetics;peroxide;peroxiredoxin;thiol oxidation;
 Language
English
 Cited by
1.
Overview on Peroxiredoxin,;

Molecules and Cells, 2016. vol.39. 1, pp.1-5 crossref(new window)
1.
Overview on Peroxiredoxin, Molecules and Cells, 2016, 39, 1, 1  crossref(new windwow)
2.
Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2, Journal of Biological Chemistry, 2017, 292, 21, 8705  crossref(new windwow)
3.
The hydrogen peroxide hypersensitivity of OxyR2 in Vibrio vulnificus depends on conformational constraints, Journal of Biological Chemistry, 2017, 292, 17, 7223  crossref(new windwow)
4.
The Conundrum of Hydrogen Peroxide Signaling and the Emerging Role of Peroxiredoxins as Redox Relay Hubs, Antioxidants & Redox Signaling, 2017  crossref(new windwow)
 References
1.
Chae, H.Z., Kim, H.J., Kang, S.W., and Rhee, S.G. (1999). Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin. Diabetes Res. Clin. Pract. 45, 101-112. crossref(new window)

2.
Cox, A.G., Pearson, A.G., Pullar, J.M., Jonsson, T.J., Lowther, W.T., Winterbourn, C., and Hampton, M.B. (2009a). Mitochondrial peroxiredoxin 3 is more resilient to hyperoxidation than cytoplasmic peroxiredoxins. Biochem. J. 421, 51-58. crossref(new window)

3.
Cox, A.G., Peskin, A.V., Paton, L.N., Winterbourn, C.C., and Hampton, M.B. (2009b). Redox potential and peroxide reactivity of human peroxiredoxin 3. Biochemistry 48, 6495-6501. crossref(new window)

4.
Hall, A., Parsonage, D., Poole, L.B., and Karplus, P.A. (2010). Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization. J. Mol. Biol. 402, 194-209. crossref(new window)

5.
Hall, A., Nelson, K., Poole, L.B., and Karplus, P.A. (2011). Structurebased insights into the catalytic power and conformational dexterity of peroxiredoxins. Antioxid. Redox Signal. 15, 795-815. crossref(new window)

6.
Hugo, M., Turell, L., Manta, B., Botti, H., Monteiro, G., Netto, L.E., Alvarez, B., Radi, R., and Trujillo, M. (2009). Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: kinetics, acidity constants, and conformational dynamics. Biochemistry 48, 9416-9426. crossref(new window)

7.
Karplus, P.A. (2015). A primer on peroxiredoxin biochemistry. Free Radic. Biol. Med. 80, 183-190. crossref(new window)

8.
Manta, B., Hugo, M., Ortiz, C., Ferrer-Sueta, G., Trujillo, M., and Denicola, A. (2009). The peroxidase and peroxynitrite reductase activity of human erythrocyte peroxiredoxin 2. Arch. Biochem. Biophys. 484, 146-154. crossref(new window)

9.
Nagy, P., Karton, A., Betz, A., Peskin, A.V., Pace, P., O'Reilly, R.J., Hampton, M.B., Radom, L., and Winterbourn, C.C. (2011). Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide: a kinetic and computational study. J. Biol. Chem. 286, 18048-18055. crossref(new window)

10.
Nakamura, T., Kado, Y., Yamaguchi, T., Matsumura, H., Ishikawa, K., and Inoue, T. (2010). Crystal structure of peroxiredoxin from Aeropyrum pernix K1 complexed with its substrate, hydrogen peroxide. J. Biochem. 147, 109-115. crossref(new window)

11.
Nelson, K.J., and Parsonage, D. (2011). Measurement of peroxiredoxin activity. Curr. Protoc. Toxicol. Chapter 7, Unit7 10.

12.
Nelson, K.J., Parsonage, D., Karplus, P.A., and Poole, L.B. (2013). Evaluating peroxiredoxin sensitivity toward inactivation by peroxide substrates. Methods Enzymol. 527, 21-40. crossref(new window)

13.
Ogusucu, R., Rettori, D., Munhoz, D.C., Netto, L.E., and Augusto, O. (2007). Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: rate constants by competitive kinetics. Free Radic. Biol. Med. 42, 326-334. crossref(new window)

14.
Parsonage, D., Youngblood, D.S., Sarma, G.N., Wood, Z.A., Karplus, P.A., and Poole, L.B. (2005). Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. Biochemistry 44, 10583-10592. crossref(new window)

15.
Parsonage, D., Nelson, K.J., Ferrer-Sueta, G., Alley, S., Karplus, P.A., Furdui, C.M., and Poole, L.B. (2015). Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC. Biochemistry 54, 1567-1575. crossref(new window)

16.
Peskin, A.V., Low, F.M., Paton, L.N., Maghzal, G.J., Hampton, M.B., and Winterbourn, C.C. (2007). The high reactivity of peroxiredoxin 2 with H(2)O(2) is not reflected in its reaction with other oxidants and thiol reagents. J. Biol. Chem. 282, 11885-11892. crossref(new window)

17.
Peskin, A.V., Cox, A.G., Nagy, P., Morgan, P.E., Hampton, M.B., Davies, M.J., and Winterbourn, C.C. (2010). Removal of amino acid, peptide and protein hydroperoxides by reaction with peroxiredoxins 2 and 3. Biochem. J. 432, 313-321. crossref(new window)

18.
Peskin, A.V., Dickerhof, N., Poynton, R.A., Paton, L.N., Pace, P.E., Hampton, M.B., and Winterbourn, C.C. (2013). Hyperoxidation of Peroxiredoxins 2 and 3: Rate constants for the reactions of the sulfenic acid of the peroxidative cysteine. J. Biol. Chem. 288, 14170-14177. crossref(new window)

19.
Peskin, A.V., Pace, P.E., Behring, J.B., Paton, L.N., Soethoudt, M., Bachschmid, M.M., and Winterbourn, C.C. (2016). Glutathionylation of the active site cysteines of peroxiredoxin 2 and recycling by glutaredoxin. J. Biol. Chem. in press.

20.
Rhee, S.G., Chae, H.Z., and Kim, K. (2005). Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic. Biol. Med. 38, 1543-1552. crossref(new window)

21.
Trujillo, M., Clippe, A., Manta, B., Ferrer-Sueta, G., Smeets, A., Declercq, J.P., Knoops, B., and Radi, R. (2007). Pre-steady state kinetic characterization of human peroxiredoxin 5: taking advantage of Trp84 fluorescence increase upon oxidation. Arch. Biochem. Biophys. 467, 95-106. crossref(new window)

22.
Trujillo, M., Ferrer-Sueta, G., and Radi, R. (2008). Kinetic studies on peroxynitrite reduction by peroxiredoxins. Methods Enzymol. 441, 173-196. crossref(new window)

23.
Winterbourn, C.C., and Hampton, M.B. (2008). Thiol chemistry and specificity in redox signaling. Free Radic. Biol. Med. 45, 549-561. crossref(new window)

24.
Winterbourn, C.C., and Hampton, M.B. (2015) Redox biology: signaling via a peroxiredoxin sensor. Nat. Chem. Biol. 11, 5-6. crossref(new window)

25.
Wood, Z.A., Poole, L.B., and Karplus, P.A. (2003). Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300, 650-653. crossref(new window)

26.
Yang, K.S., Kang, S.W., Woo, H.A., Hwang, S.C., Chae, H.Z., Kim, K., and Rhee, S.G. (2002). Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J. Biol. Chem. 277, 38029-38036. crossref(new window)