Сравнительное исследование механизмов взаимодействия цитохрома Р450 2В4 и гемового домена монооксигеназы Р450ВМ3 с их партнерами-донорами электронов

6. Выводы.

1. В образовании функционально-активного комплекса переноса электронов между цитохромом Р450 2В4 и NADPH-зависимой цитохром Р450 редуктазой важную роль играют электростатические взаимодействия, которые могут быть описаны как взаимодействие двух противоположно заряженных центров связывания радиусом 8 А и, предположительно, сопровождаются образованием 3−4 солевых мостиков.

2. Гемовый и флавиновый домены Р450ВМЗ характеризуются достаточно низким сродством друг к другу (Kd = 3.5 цМ), причём взаимодействия между ними затруднено некоторым электростатическим отталкиванием, которое может быть описано как взаимодействие двух одинаково заряженных участков диаметром 6.5 А.

3. Компоненты микросомальной и бактериальной МОС взаимодействуют между собой с образованием функционально-активных смешанных комплексов. Различия между ММО и Р450ВМЗ во вкладе электростатических взаимодействий в образование комплекса переноса электрона обусловлены, прежде всего, особенностями структур 2В4 и BMP.

4. Скорость переноса электронов в комплексах цитохрома Р450 2В4 и гемового домена Р450ВМЗ с микросомальной редуктазой и BMR определяется природой флавопротеина. BMR является более эффективным донором электронов как для 2В4, так и для BMP.

5. Разработан новый подход для изучения структурных изменений в белках при комплексообразовании методом ИК-спектроскопии с преобразованием Фурье. Его применение в исследовании белок-белковых взаимодействий в МОС показало, что образование комплекса BMP с FMND сопровождается формированием солевого мостика His-Glu и разрывом внутримолекулярного солевого мостика с участием остатка тирозина, а также заметными конформационными переходами в молекулах обоих белков.

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