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Kinetics of CO binding to H+-motive oxidases of the caa3-type from Bacillus FTU and of the o-type from Escherichia coliстатья
Информация о цитировании статьи получена из
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Дата последнего поиска статьи во внешних источниках: 20 января 2021 г.
- Авторы: Muntyan M.S., Bloch D.A., Ustiyan V.S., Drachev L.A.
- Журнал: FEBS Letters
- Том: 327
- Номер: 3
- Год издания: 1993
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 351
- Последняя страница: 354
- DOI: 10.1016/0014-5793(93)81019-V
- Аннотация: The kinetics of CO rebinding with isolated Bacillus FTU caa3-type oxidase and with solubilized Escherichia coli membranes (GO103 strain) containing the o-type oxidase as the main O2-reducing enzyme were studied under reducing conditions by laser flash photolysis of the CO-oxidase complexes. The spectra of the optical absorbance changes upon photolysis were characteristic of CO-caa3- and CO-o-oxidase complexes in Bac. FTU and E. coli, respectively. Small quantities of d-type oxidase in E. coli GO103 membranes were detected. The kinetics of CO reassociation with reduced caa3- and o-type oxidases were monophasic with tau 25-30 ms in both cases.
- Добавил в систему: Мунтян Мария Сергеевна