БИОХИМИЯ, 2018, том 83, вып. 10, с. 1427–1449

УДК 577.151.644

АДФ-ингибирование H+-F0F1-АТФ синтазы

Обзор

© 2018 А.С. Лапашина 1,2, Б.А. Фенюк 1,2

1 Московский государственный университет им. М.В. Ломоносова, факультет биоинженерии и биоинформатики, 119991 Москва, Россия

2 Московский государственный университет им. М.В. Ломоносова, НИИ физико-химической биологии им. А.Н. Белозерского, 119991 Москва, Россия; электронная почта: feniouk@fbb.msu.ru

Поступила в редакцию 06.12.2017
После доработки 08.06.2018

DOI: 10.1134/S0320972518100019

КЛЮЧЕВЫЕ СЛОВА: АТФ синтаза, F-АТФаза, АДФ-ингибирование, регуляция, F0F1.

Аннотация

H+-F0F1-АТФ синтаза (F-АТФаза, АТФаза F-типа, F0F1-комплекс) катализирует синтез АТФ из АДФ и неорганического фосфата в эубактериях, митохондриях, хлоропластах и некоторых архебактериях. Синтез АТФ сопряжен с транспортом протонов через мембранную часть фермента под действием протон-движущей силы, создаваемой ферментами дыхательной и фотосинтетической цепи переноса электронов. При снижении или исчезновении протон-движущей силы (де-энергизация) АТФ синтаза способна катализировать обратную реакцию, работая как АТФ-зависимый протонный насос. АТФазная активность фермента регулируется несколькими различными механизмами, из которых наиболее консервативным является неконкурентное ингибирование комплексом MgАДФ (АДФ-ингибирование). Если в каталитическом сайте оказывается АДФ в отсутствии фосфата, это может привести к конформационным изменениям, блокирующим выход АДФ и полностью инактивирующим фермент. Высвобождение прочно связанного АДФ и ре-активация АТФ синтазы может происходить под действием протон-движущей силы, причем пороговое значение для ре-активации может быть выше такового для синтеза АТФ. Кроме того, энергизация мембраны увеличивает аффинность каталитического сайта к фосфату, тем самым, снижая вероятность нахождения в сайте АДФ без фосфата и препятствуя переходу фермента в АДФ-инактивированное состояние. Помимо фосфата, некоторые соединения, в том числе, спирты, сульфит и бикарбонат, лаурилдиметиламиноксид (LDAO) и ряд других детергентов также способны ослаблять АДФ-ингибирование и увеличивать АТФазную активность фермента. В обзоре представлена информация по АДФ-ингибированию АТФ синтаз из разных организмов, обсуждается роль этого явления in vivo и его взаимосвязь с другими регуляторными механизмами — ингибированием АТФазной активности субъединицей эпсилон и связыванием нуклеотидов в некаталитических сайтах фермента. Cледует отметить, что в ферменте из Escherichia coli АДФ-ингибирование выражено слабо и не снижается фосфатом.

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Вклад авторов

Авторы внесли одинаковый вклад в представленную работу.

Финансирование

Работа выполнена при финансовой поддержке РНФ (проект 14-14-00128 «Молекулярные механизмы преобразования энергии при бактериальном окислительном фосфорилировании»).

Благодарности

Авторы благодарят анонимных рецензентов за ценные замечания при написании обзора.

Конфликт интересов

Авторы заявляют, что у них нет конфликта интересов.

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