کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1942079 | 1537040 | 2015 | 29 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The Carbon Monoxide Dehydrogenase from Desulfovibrio vulgaris
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کلمات کلیدی
ACSCODHMoorella thermoaceticaCarboxydothermus hydrogenoformansDesulfovibrio vulgarisEscherichia coli - اشریشیا کُلیProtein purification - خالصسازی یا تخلیص پروتئینSodium dithionite - دی اتینیت سدیمElectron paramagnetic resonance (EPR) - رزونانس پارامغناطیسی الکترون (EPR)Acetyl-CoA synthase - سیترات استیل کوآEnzyme kinetics - سینتیک آنزیمRhodospirillum rubrum - قرمز ریکتزیاCarbon monoxide dehydrogenase - مونوکسید کربن دهیدروژناز
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Ni-containing Carbon Monoxide Dehydrogenases (CODHs) catalyze the reversible conversion between CO and CO2 and are involved in energy conservation and carbon fixation. These homodimeric enzymes house two NiFeS active sites (C-clusters) and three accessory [4Fe-4S] clusters. The Desulfovibrio vulgaris (Dv) genome contains a two-gene CODH operon coding for a CODH (cooS) and a maturation protein (cooC) involved in nickel insertion in the active site. According to the literature, the question of the precise function of CooC as a chaperone folding the C-cluster in a form which accommodates free nickel or as a mere nickel donor is not resolved. Here, we report the biochemical and spectroscopic characterization of two recombinant forms of the CODH, produced in the absence and in the presence of CooC, designated CooS and CooSC, respectively. CooS contains no nickel and cannot be activated, supporting the idea that the role of CooC is to fold the C-cluster so that it can bind nickel. As expected, CooSC is Ni-loaded, reversibly converts CO and CO2, displays the typical Cred1 and Cred2 EPR signatures of the C-cluster and activates in the presence of methyl viologen and CO in an autocatalytic process. However, Ni-loaded CooSC reaches maximum activity only upon reductive treatment in the presence of exogenous nickel, a phenomenon that had not been observed before. Surprisingly, the enzyme displays the Cred1 and Cred2 signatures whether it has been activated or not, showing that this activation process of the Ni-loaded Dv CODH is not associated with structural changes at the active site.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1847, Issue 12, December 2015, Pages 1574-1583
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1847, Issue 12, December 2015, Pages 1574-1583
نویسندگان
Jessica Hadj-Saïd, Maria-Eirini Pandelia, Christophe Léger, Vincent Fourmond, Sébastien Dementin,