کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1925809 1536418 2011 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies
چکیده انگلیسی

This review describes the use of cryoreduction/annealing EPR/ENDOR techniques for determining the active oxidizing species in reactions catalyzed by heme monooxygenases. The three candidate heme states are: ferric peroxo, ferric hydroperoxo and compound I intermediates. The enzymes discussed include cytochromes P450, nitric oxide synthase and heme oxygenase.

Research highlights
► EPR/ENDOR spectroscopy of radiolytically cryoreduced oxyheme monooxygenases has identified the active oxidizing species in: (1) cytochrome P450 reactions; (2) the two stages by which NOS generates NO; (3) meso-heme hydroxylation by heme oxygenases.
► It has also demonstrated the influence of substrate in modulating monooxygenase activity.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 507, Issue 1, 1 March 2011, Pages 36–43
نویسندگان
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