Recombinant Cu,Zn Superoxide Dismutase from Caulobacter crescentus has been expressed in Escherichia coli and characterized. The corresponding recombinant protein has a molecular weight typical of a homodimeric Cu,ZnSODs and an activity comparable to that of other prokaryotic enzymes. The copper active site is characterized by a peculiar axial geometry as evidenced by its electron paramagnetic resonance spectrum, moreover, the copper atom displays a low accessibility toward external chelating agents indicating a lower solvent accessibility when compared to other prokaryotic enzymes. Investigation of the enzyme thermal stability through differential scanning calorimetry indicates the occurrence of two transitions at low and higher temperature that are found to be due to the apo and holo protein, respectively, confirming that the metals have a crucial role in the stabilization of this class of enzymes. (c) 2005 Elsevier B.V. All rights reserved.

De Domenico, I., Lania, A., Bonaccorsi_di_patti, M.c., Battistoni, A., Musci, G., Desideri, A. (2006). Purification and characterization of recombinant Caulobacter crescentus Cu,Zn superoxide dismutase. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1764(1), 105-109 [10.1016/j.bbapap.2005.08.021].

Purification and characterization of recombinant Caulobacter crescentus Cu,Zn superoxide dismutase

BATTISTONI, ANDREA;DESIDERI, ALESSANDRO
2006-01-01

Abstract

Recombinant Cu,Zn Superoxide Dismutase from Caulobacter crescentus has been expressed in Escherichia coli and characterized. The corresponding recombinant protein has a molecular weight typical of a homodimeric Cu,ZnSODs and an activity comparable to that of other prokaryotic enzymes. The copper active site is characterized by a peculiar axial geometry as evidenced by its electron paramagnetic resonance spectrum, moreover, the copper atom displays a low accessibility toward external chelating agents indicating a lower solvent accessibility when compared to other prokaryotic enzymes. Investigation of the enzyme thermal stability through differential scanning calorimetry indicates the occurrence of two transitions at low and higher temperature that are found to be due to the apo and holo protein, respectively, confirming that the metals have a crucial role in the stabilization of this class of enzymes. (c) 2005 Elsevier B.V. All rights reserved.
2006
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
superoxide dismutase; Caulobacter crescentus; copper
De Domenico, I., Lania, A., Bonaccorsi_di_patti, M.c., Battistoni, A., Musci, G., Desideri, A. (2006). Purification and characterization of recombinant Caulobacter crescentus Cu,Zn superoxide dismutase. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1764(1), 105-109 [10.1016/j.bbapap.2005.08.021].
De Domenico, I; Lania, A; Bonaccorsi_di_patti, Mc; Battistoni, A; Musci, G; Desideri, A
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/37949
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