کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1926352 | 1536454 | 2009 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Thermal stability and redox properties of M. tuberculosis CuSOD
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
SODCAntioxidant enzymes - آنزیم های آنتی اکسیدانamyotrophic lateral sclerosis - اسکلروز جانبی آمیوتروفیکConformational stability - ثبات سازگاریSuperoxide dismutase - سوکسوکس دیسموتازZinc - فلز رویMycobacterium tuberculosis - مایکوباکتریوم توبرکلوزیسCopper - مسZinc homeostasis - هومئوستاز رویDifferential scanning calorimetry - کالریمتری روبشی افتراقی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Thermal stability and redox properties of M. tuberculosis CuSOD Thermal stability and redox properties of M. tuberculosis CuSOD](/preview/png/1926352.png)
چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 486, Issue 2, 15 June 2009, Pages 119-124
Journal: Archives of Biochemistry and Biophysics - Volume 486, Issue 2, 15 June 2009, Pages 119-124
نویسندگان
Melania D'Orazio, Laura Cervoni, Anna Giartosio, Giuseppe Rotilio, Andrea Battistoni,