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Трансгидрогеназная активность митохондриального Комплекса I и его нуклеотид-связывающие центры

Диссертация: Трансгидрогеназная активность митохондриального Комплекса I и его нуклеотид-связывающие центры
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Свойства нуклеотид-связывающего активного центра (ов) Комплекса I мало изучены. До последнего времени считалось общепринятым, что фермент имеет единственный центр специфичного связывания NADH и/или NAD+, ассоциированный с его 51 кДа флавин-содержащей субъединицей. Однако, ряд данных указывает на существование более чем одного центра связывания нуклеотидов в составе Комплекса I. Такие данные… Читать ещё >

Трансгидрогеназная активность митохондриального Комплекса I и его нуклеотид-связывающие центры (реферат, курсовая, диплом, контрольная)

Содержание

  • СПИСОК СОКРАЩЕНИЙ ОБЗОР ЛИТЕРАТУРЫ
  • 1. Структура протон-транслоцирующих
  • ЛАОНгхинон оксидоредуктаз
    • 1. 1. Субъединицы
  • Субъединичный состав митохондриальных и бактериальных ферментов Субкомплексы
  • Ассоциация субъединиц в процессе сборки
  • Комплекса I Происхождение субъединиц и эволюция
  • Комплекса I МАБН-дегидрогеназы, нетранслоцирующие протоны
    • 1. 2. Редокс компоненты
  • Железо-серные центры Хиноны
  • 2. Каталитические свойства митохондриальной
  • NADH:yбиxинoн оксидоредуктазы
    • 2. 1. Препараты ЫАБН-дегидрогеназы СМЧ
  • Комплекс I БР
    • 2. 2. Реакции, катализируемые Комплексом I ЫАБН-оксидазная реакция
  • — Дыхательный контроль
  • — Обратимая деактивация Комплекса I Обратный перенос электронов
  • Окисление ЫАБН искусственными акцепторами электронов
  • — Аналоги и гомологи убихинона
  • — Феррицианид и гексаминорутений Генерация супероксид аниона Трансгидрогеназная реакция
  • — Комплекс I
  • — Н^-трансгидрогеназа
    • 2. 3. Транслокация протонов
    • 2. 4. Ингибиторы Комплекса I
  • Ингибиторы центров связывания нуклеотидов и начальных этапов переноса электронов
  • — NAD+, NADH, ADP-рибоза и их производные
  • — Рейн
  • — Тинопалы 42 Ингибиторы восстановления хинонов
  • — Ротенон
  • — Пиерицидин А
  • — Ацетогенины
  • — Антибиотики миксобактерий
  • — Другие ингибиторы
  • 3. Активный центр NADH: y6nximoH оксидоредуктазы
    • 3. 1. Центры связывания нуклеотидов 47 Субъединица 51 кДа 47 Субъединица 39 кДа 48 Субъединицы, метящиеся фотоаффинными аналогами нуклеотидов
    • 3. 2. Участие центров связывания нуклеотидов в реакциях Комплекса I 49 Указания на работу не менее двух центров связывания нуклеотидов 49 Подходы к определению количества субстрат-связывающих мест
  • МЕТОДЫ ИССЛЕДОВАНИЯ
  • 1. Препаративные методы
    • 1. 1. Выделение митохондрий из сердца быка
    • 1. 2. Получение субмитохондриальных частиц (СМЧ)
    • 1. 3. Выделение ЫА1) Н:убихинон оксидоредуктазы из митохондрий
  • Промывание митохондрий
  • Получение препарата S1 (Комплексы I, II и III)
  • Получение препарата R4B (Комплексы I и III)
  • Выделение NADH: y6nxHHOH оксидоредуктазы
    • 1. 4. Фракционирование Комплекса I, выделение трехсубъединичного флавопротеина (FP)
    • 1. 5. Обработка СМЧ трипсином
    • 1. 6. Сопряжение СМЧ олигомицином
    • 1. 7. Получение APADH
  • 2. Аналитические методы
    • 2. 1. Реакции, катализируемые препаратами
  • NADH-дегидрогеназы
  • NADH-оксидазная реакция, дыхательный контроль (ДК)
  • Сукцинат-зависимый обратный перенос электронов
  • DD трансгидрогеназная реакция
    • 2. 2. Определение концентрации APAD+ и NAD+
    • 2. 3. Преинкубация Комплекса I с NADH
    • 2. 4. Экстракция нуклеотидов 63 Экстракция NAD+ и флавинов хлорной кислотой 63 Экстракция флавинов трихлоруксусной кислотой (ТХУ) 63 Щелочная экстракция NADH
    • 2. 5. Регистрация Ар, н+
    • 2. 6. Кинетическое определение механизма бисубстратной реакции
  • Тройной комплекс и двойное замещение 65 Последовательность взаимодействия субстратов с ферментом в реакциях, протекающих с образованием тройного комплекса
  • РЕЗУЛЬТАТЫ
  • 1. NADH:y6HXHHOH оксидоредуктаза и DD трансгидрогеназная активность СМЧ
  • 2. Кинетический механизм DD трансгидрогеназной реакции, катализируемой NADH: y6nxnHOH оксидоредуктазой
    • 2. 1. СМЧ 70 NADH-«APAD+ реакция 70 APADH-«NAD+ реакция
    • 2. 2. Комплекс I
    • 2. 3. FP
    • 2. 4. Содержание связанных нуклеотидов в составе Комплекса I
  • 3. Окисление и восстановление нуклеотидов в реакциях прямого и обратного переноса электронов, катализируемых Комплексом I
  • 4. Влияние обратимых ингибиторов активного центра
  • Комплекса I на DD трансгидрогеназную реакцию
    • 4. 1. ADP-рибоза
    • 4. 2. Рейн
    • 4. 3. NAD+
    • 4. 4. Тинопалы (AMS-GX, 5BM-GX) 95 Влияние тинопалов на спектры поглощения
  • NADHhAPADH 96 Влияние AMS-GX и 5BM-GX на DD реакцию
  • Комплекса I
  • 5. DD трансгидрогеназная реакция 1 и A|uH+
  • ОБСУЖДЕНИЕ
  • ВЫВОДЫ

NADH:y6nxHHOH оксидоредуктаза (Комплекс I, NADH-дегидрогеназа, КФ 1.6.5.3) — чрезвычайно сложный компонент дыхательной цепи митохондрий. Фермент катализирует окисление NADH убихиноном, сопряженное с векторным переносом 4 протонов из матрикса митохондрий в межмембранное пространство. Комплекс I построен не менее чем из 41 субъединиц (общая молекулярная масса — порядка 1 ООО ООО Да) и содержит FMN, 5−7 железосерных кластеров и связанный убихинон.

Свойства нуклеотид-связывающего активного центра (ов) Комплекса I мало изучены. До последнего времени считалось общепринятым, что фермент имеет единственный центр специфичного связывания NADH и/или NAD+, ассоциированный с его 51 кДа флавин-содержащей субъединицей. Однако, ряд данных указывает на существование более чем одного центра связывания нуклеотидов в составе Комплекса I. Такие данные кратко суммированы ниже:

1) Fe-S кластеры фермента по-разному восстанавливаются при добавлении NADH или NADPH;

2) кинетика генерации супероксид-радикала характеризуется двумя значениями Кт как для NADH, так и для NADPH;

3) в зависимости от концентрации, NAD+ влияет как конкурентный или неконкурентный ингибитор по отношению к NADH;

4) фотоаффинные аналоги субстратов включаются в несколько субъединиц фермента;

5) сродство фермента к NAD+ и NADH в реакциях окисления NADH и А|Ын±зависимого восстановления NAD+ убихиноном существенно различается;

6) ADP-рибоза конкурирует с NADH в прямой реакции и не влияет на обратный перенос электронов. 8.

Таким образом, мы полагаем, что количество центров связывания нуклеотидов остается неизвестным. Способность Комплекса I катализировать трансгидрогеназную реакцию предоставляет одну из возможностей для изучения нуклеотид-связывающих свойств фермента. Кинетическое исследование этой бисубстратной реакции может служить, хотя и косвенным, но достаточно надежным инструментом для этой цели.

В настоящей работе в качестве инструмента исследования свойств активного центра (ов) Комплекса I была использована NADH—>АРАБ+ (3-ацетилпиридин аденин динуклеотид) трансгидрогеназная реакция, катализируемая тремя препаратами ЫАОН: дегидрогеназы: субмитохондриальными частицами (СМЧ), изолированным Комплексом I и его трехсубъединичным фрагментом БР. Полученные результаты позволяют считать, что фермент содержит не менее трех функционально значимых центров связывания субстратов-нуклеотидов.

ОБЗОР ЛИТЕРАТУРЫ.

выводы.

1. Показано, что митохондриальная NADH.-убихинон оксидоредуктаза катализирует две NADH-«APAD+ (DD) трансгидрогеназные реакции, отличающиеся по скоростям, кинетическому механизму, сродству к субстратам и чувствительности к Ацн+.

2. Установлено, что реакция 1 протекает по упорядоченному механизму с образованием тройного комплекса, с участием двух нуклеотид-связывающих центров. Оба центра входят в состав трехсубъединичного флавопротеина (FP). NADH является первым субстратом. Для реакции характерно двойное субстратное ингибирование при концентрациях субстратов, на порядок привышающих Кт. Реакция ингибируется при энергизации мембраны.

3. В DD реакции 1 восстановленный нуклеотид связывается в том же центре, что и в NADH-оксидазной реакции. Центр связывания окисленного нуклеотида в реакции 1 идентичен субстрат-связывающему центру в реакции обратного переноса электронов.

4. Реакция 2 протекает по механизму двойного замещения («пинг-понг») и, в сравнении с реакцией 1, характеризуется на порядок более высокой скоростью и на порядок более низким сродством к окисленому нуклеотиду. Реакция не чувствительна к Ацн+.

5. В обеих реакциях NAD+ конкурирует с APAD+ и не конкурирует с NADH.

6. ADP-рибоза и реин по разному ингибируют две реакции, катализируемые нативным ферментом.

7. Заключено, что в реакции 2 функционирует отдельный нуклеотид-связывающий центр (ы), отличный от двух субстрат связывающих центров участвующих в реакции 1. Таким образом, в составе.

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