کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10565230 | 971598 | 2005 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Dioxygen activation by copper, heme and non-heme iron enzymes: comparison of electronic structures and reactivities
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی (عمومی)
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چکیده انگلیسی
Enzymes containing heme, non-heme iron and copper active sites play important roles in the activation of dioxygen for substrate oxidation. One key reaction step is CH bond cleavage through H-atom abstraction. On the basis of the ligand environment and the redox properties of the metal, these enzymes employ different methods of dioxygen activation. Heme enzymes are able to stabilize the very reactive iron(IV)-oxo porphyrin-radical intermediate. This is generally not accessible for non-heme iron systems, which can instead use low-spin ferric-hydroperoxo and iron(IV)-oxo species as reactive oxidants. Copper enzymes employ still a different strategy and achieve H-atom abstraction potentially through a superoxo intermediate. This review compares and contrasts the electronic structures and reactivities of these various oxygen intermediates.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Current Opinion in Chemical Biology - Volume 9, Issue 2, April 2005, Pages 152-163
Journal: Current Opinion in Chemical Biology - Volume 9, Issue 2, April 2005, Pages 152-163
نویسندگان
Andrea Decker, Edward I Solomon,