معقدات الحديد الثنائي مع مرتبطات عطرية مستبدلة الموقع (α) من نمط ثلاثي (٢-بيرديل ميثيل) امين: تأثير المتبادلات والفعالية بالمحاكاة البيولوجية.
Abstract
تؤدي المحاكاة البيولوجية لعملية الاكسدة للمواقع الفعالة لبروتينات الحديد إلى تشكل فوق الاكاسيد وبشكل محدد الماء الأكسيجيني حيث يمثل الأخير عامل مؤكسد قوي ومرضي الى حد بعيد ويتميز بعدم السمية وبالتكلفة المنخفضة. في العديد من الحالات توظف الطبيعة الأكسجين الجزيئي لعمليات الاكسدة وبشكل خاص تحت شروط ساحبة. تمت دراسة معقدات الحديد مع المرتبطات من نمط تريس (٢-بيرديل ميثيل) امين للمحاكاة البيولوجية للمواقع الفعالة حيويا واثبتت أهميتها الحيوية. يدرس هذا البحث إمكانية الحصول على معقدات الحديد الثنائي مع مرتبطات عطرية من نمط ثلاثي (٢-بيرديل ميثيل) امين على الموقع ألفا من ذرة الآزوت مع اختبار الفعالية تجاه الأكسيجين الجزيئي لمعقد واحد تم اختياره من المعقدات المصنعة. Biomimetic oxidations at active sites of iron proteins involve peroxides, especially hydrogen peroxide which is a strong and very convenient reagent since it is inexpensive and does not release any toxic by-products. In many cases however, mother Nature uses molecular dioxygen to carry out major oxidation reactions in particularly attractive conditions. The biomimetic interest of iron complexes in the tris(2-pyridylmethyl)amine series TPA is no longer to demonstrate. We prepared various α-substituted TPA-based ligands with the idea to modulate the electronic properties at the metal centre. We then checked the reactivity of a one example of complexes towards molecular dioxygen.Downloads
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