Thermodynamics of the dimer-decamer transition of reduced human and plant 2-Cys peroxiredoxin

Barranco-Medina S, Kakorin S, Lazaro JJ, Dietz K-J (2008)
BIOCHEMISTRY 47(27): 7196-7204.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
Isothermal titration calorimetry (ITC) is a powerful technique for investigating self-association processes of protein complexes and was expected to reveal quantitative data on., peroxiredoxin oligomerization by directly measuring the thermodynamic parameters of dimer-dimer interaction. Recombinant classical 2-cysteine peroxoredoxins from Homo sapiens, Arabidopsis thaliana, and Pisum sativum as well as a carboxy-terminally truncated variant were subjected to ITC analysis by stepwise injection into the reaction vessel under various redox conditions. The direct measurement of the decamer-dimer equilibrium of reduced peroxiredoxin revealed a critical concentration in the very low micromolar range. The data suggest a cooperative assembly above this critical transition concentration where a nucleus facilitates assembly. The rather abrupt transition indicates that assembly processes do not occur below the critical transition concentration while oligomerization is efficiently triggered above it. The magnitude of the measured enthalpy confirmed the endothermic nature of the peroxiredoxin oligomerization. Heterocomplexes between peroxiredoxin polypeptides from different species were not formed. We conclude that a functional constraint conserved the dimer-decamer transition with highly similar critical transition concentrations despite emerging sequence variation during evolution.
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BIOCHEMISTRY
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47
Zeitschriftennummer
27
Seite
7196-7204
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Barranco-Medina S, Kakorin S, Lazaro JJ, Dietz K-J. Thermodynamics of the dimer-decamer transition of reduced human and plant 2-Cys peroxiredoxin. BIOCHEMISTRY. 2008;47(27):7196-7204.
Barranco-Medina, S., Kakorin, S., Lazaro, J. J., & Dietz, K. - J. (2008). Thermodynamics of the dimer-decamer transition of reduced human and plant 2-Cys peroxiredoxin. BIOCHEMISTRY, 47(27), 7196-7204. doi:10.1021/bi8002956
Barranco-Medina, S., Kakorin, S., Lazaro, J. J., and Dietz, K. - J. (2008). Thermodynamics of the dimer-decamer transition of reduced human and plant 2-Cys peroxiredoxin. BIOCHEMISTRY 47, 7196-7204.
Barranco-Medina, S., et al., 2008. Thermodynamics of the dimer-decamer transition of reduced human and plant 2-Cys peroxiredoxin. BIOCHEMISTRY, 47(27), p 7196-7204.
S. Barranco-Medina, et al., “Thermodynamics of the dimer-decamer transition of reduced human and plant 2-Cys peroxiredoxin”, BIOCHEMISTRY, vol. 47, 2008, pp. 7196-7204.
Barranco-Medina, S., Kakorin, S., Lazaro, J.J., Dietz, K.-J.: Thermodynamics of the dimer-decamer transition of reduced human and plant 2-Cys peroxiredoxin. BIOCHEMISTRY. 47, 7196-7204 (2008).
Barranco-Medina, Sergio, Kakorin, Sergej, Lazaro, Juan Jose, and Dietz, Karl-Josef. “Thermodynamics of the dimer-decamer transition of reduced human and plant 2-Cys peroxiredoxin”. BIOCHEMISTRY 47.27 (2008): 7196-7204.

30 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Typical 2-Cys peroxiredoxins--structures, mechanisms and functions.
Hall A, Karplus PA, Poole LB., FEBS J 276(9), 2009
PMID: 19476488
Typical 2-Cys peroxiredoxins--modulation by covalent transformations and noncovalent interactions.
Aran M, Ferrero DS, Pagano E, Wolosiuk RA., FEBS J 276(9), 2009
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The oligomeric conformation of peroxiredoxins links redox state to function.
Barranco-Medina S, Lázaro JJ, Dietz KJ., FEBS Lett 583(12), 2009
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Hexameric oligomerization of mitochondrial peroxiredoxin PrxIIF and formation of an ultrahigh affinity complex with its electron donor thioredoxin Trx-o.
Barranco-Medina S, Krell T, Bernier-Villamor L, Sevilla F, Lázaro JJ, Dietz KJ., J Exp Bot 59(12), 2008
PMID: 18632730

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