کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10574029 | 976488 | 2005 | 18 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Heme oxygenase, steering dioxygen activation toward heme hydroxylation
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی معدنی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The activation of dioxygen by heme oxygenase proceeds via formation of an obligatory ferric hydroperoxide intermediate (FeIII-OOH), as is the case in the activation of dioxygen by monooxygenase enzymes. This review summarizes current understanding of the structural and dynamic properties in heme oxygenase that channel the reactivity of the FeIII-OOH intermediate toward heme hydroxylation rather than oxoferryl formation. In addition, structural and electronic factors dictating the regiospecificity of heme oxygenation are analyzed in the context of recent X-ray and NMR spectroscopic studies. Differences in mechanism between heme hydroxylation, as carried out by heme oxygenase, and the coupled oxidation process, are also addressed.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Inorganic Biochemistry - Volume 99, Issue 1, January 2005, Pages 337-354
Journal: Journal of Inorganic Biochemistry - Volume 99, Issue 1, January 2005, Pages 337-354
نویسندگان
Mario Rivera, Yuhong Zeng,