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Spin control of oxidative phosphorylationтезисы доклада
- Авторы: Skorobogatova Y.A., Nesterov S.V., Yaguzhinskiy L.S.
- Сборник: Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Серия: Supplement 2014 EBEC abstracts
- Том: 1837
- Тезисы
- Год издания: 2014
- Издательство: ELSEVIER SCIENCE BV
- Местоположение издательства: PO BOX 211, AMSTERDAM, NETHERLANDS, 1000 AE
- Первая страница: e31
- Последняя страница: e32
- DOI: 10.1016/j.bbabio.2014.05.292
- Аннотация: According to our previous investigations [1], under conditions of low-amplitude mitochondrial swelling (in hypotonic medium, 120 mOsm) electron transport chain and ATPase system operate as a tightly coupled supercomplex. The temperature-dependent efficiency of the mitochondrial oxidative phosphorylation was measured within 15–36 °С. Abnormally narrow peak of the parameter ADP/O was detected at 19 ± 1 °С. This finding suggests the existence of highly organized process that controls ATP synthesis. The effect could not be explained in terms of classical biochemical kinetics. The temperature dependence of pyrene-induced quenching of tryptophan fluorescence in the mitochondrial membrane-bound proteins revealed their conformational transition observed under the conditions facilitating supercomplex formation at the same narrow temperature range of 19 ± 2 °С [2]. This abnormal range of both (functional and structural) temperature dependencies coincides exactly with the point where the conversion of two distinct quantum states of water (ortho–para water differs in their mutual hydrogen spin orientation) is facilitated [3]. These spin-isomers of water were recently discovered experimentally [4], including a liquid water phase [5]. We explain narrow temperaturedependent effects as a phenomenon based on strongly different affinities [6] of ortho–para isomers of water to the proteins involved in oxidative phosphorylation.
- Добавил в систему: Ягужинский Лев Сергеевич