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Thermal stability and redox properties of M. tuberculosis CuSOD.

Abstract：

:The superoxide dismutase from Mycobacterium tuberculosis is the only Cu-containing superoxide dismutase that lacks zinc in the active site. To explore the structural properties of this unusual enzyme, we have investigated its stability by differential scanning calorimetry. We have found that the holo-enzyme is significantly more stable than the apo-protein or the partially metallated enzyme, but that its melting temperature is markedly lower than that of all the other characterized eukaryotic and prokaryotic Cu,Zn superoxide dismutases. We have also observed that, unlike the zinc-free eukaryotic or bacterial enzymes, the active site copper of the mycobacterial enzyme is not reduced by ascorbate, confirming that its redox properties are comparable to those typical of the enzymes containing zinc in the active site. Our findings highlight the role of zinc in conferring stability to Cu,Zn superoxide dismutases and indicate that the structural rearrangements observed in M. tuberculosis Cu,SOD compensate for the absence of zinc in achieving a fully active enzyme.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

D'Orazio M,Cervoni L,Giartosio A,Rotilio G,Battistoni A

doi

10.1016/j.abb.2009.04.005

subject

Has Abstract

pub_date

2009-06-15 00:00:00

pages

119-24

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(09)00122-2

journal_volume

486

pub_type

杂志文章

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