کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10768140 | 1050804 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Kinetic and spectroscopic investigation of CoII, NiII, and N-oxalylglycine inhibition of the FeII/α-ketoglutarate dioxygenase, TauD
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Kinetic and spectroscopic investigation of CoII, NiII, and N-oxalylglycine inhibition of the FeII/α-ketoglutarate dioxygenase, TauD Kinetic and spectroscopic investigation of CoII, NiII, and N-oxalylglycine inhibition of the FeII/α-ketoglutarate dioxygenase, TauD](/preview/png/10768140.png)
چکیده انگلیسی
CoII, NiII, and N-oxalylglycine (NOG) are well-known inhibitors of FeII/α-ketoglutarate (αKG)-dependent hydroxylases, but few studies describe their kinetics and no spectroscopic investigations have been reported. Using taurine/αKG dioxygenase (TauD) as a paradigm for this enzyme family, time-dependent inhibition assays showed that CoII and NiII follow slow-binding inhibition kinetics. Whereas NiII-substituted TauD was non-chromophoric, spectroscopic studies of the CoII-substituted enzyme revealed a six-coordinate site (protein alone or with αKG) that became five-coordinate upon taurine addition. The CoII spectrum was not perturbed by a series of anions or oxidants, suggesting the CoII is inaccessible and could be used to stabilize the protein. NOG competed weakly (Ki â¼Â 290 μM) with αKG for binding to TauD, with the increased electron density of NOG yielding electronic transitions for NOG-FeII-TauD and taurine-NOG-FeII-TauD at 380 nm (ε380 90-105 Mâ1 cmâ1). The spectra of the NOG-bound TauD species did not change significantly upon oxygen exposure, arguing against the formation of an oxygen-bound state mimicking an early intermediate in catalysis.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 338, Issue 1, 9 December 2005, Pages 191-197
Journal: Biochemical and Biophysical Research Communications - Volume 338, Issue 1, 9 December 2005, Pages 191-197
نویسندگان
Efthalia Kalliri, Piotr K. Grzyska, Robert P. Hausinger,