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Redox-linked protolytic reactions in soluble cytochrome-c oxidase from beaf-heart mitochondria: redox Bohr effectsстатья
Информация о цитировании статьи получена из
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Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 27 декабря 2018 г.
- Авторы: Capitanio N., Vygodina T.V., Capitanio G., Konstantinov A., Nicholls P., Papa S.
- Журнал: Biochimica et Biophysica Acta - Bioenergetics
- Том: 1318
- Номер: 1
- Год издания: 1997
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 255
- Последняя страница: 265
- DOI: 10.1016/S0005-2728(96)00143-0
- Аннотация: A study is presented of co-operative redox-linked protolytic reactions (redox Bohr effects) in soluble cytochrome-c oxidase purified from bovine-heart mitochondria. Bohr effects were analyzed by direct measurement, with accurate spectrophotometric and potentiometric methods, of H+ uptake and release by the oxidase associated with reduction and oxidation of hemes a and a3. CuA and CuB in the unliganded and in the CN- or CO-liganded enzyme. The results show that there are in the bovine oxidase four protolytic groups undergoing reversible pK shifts upon oxido-reduction of the electron transfer metals. Two groups with pKox and pKred values around 7 and > 12 respectively appear to be linked to redox transitions of heme a3. One group with pKox and pKred around 6 and 7 is apparently linked to CuB, a fourth one with pKox and pKred of 6 and 9 appears to be linked to heme a. The possible nature of the amino acids involved in the redox Bohr effects and their role in H+ translocation is discussed.
- Добавил в систему: Выгодина Татьяна Владимировна