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The respiratory nitric oxide reductase (NorBC) from Paracoccus denitrificans. Reviewстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 27 февраля 2017 г.
- Авторы: Field S.J., Thorndycroft F.H., Matorin A.D., Richardson D.J., Watmough N.J.
- Журнал: Methods in Enzymology
- Том: 437
- Год издания: 2008
- Издательство: Academic Press
- Местоположение издательства: United States
- Первая страница: 79
- Последняя страница: 101
- DOI: 10.1016/S0076-6879(07)37005-5.
- Аннотация: Abstract The two subunit cytochrome bc complex (NorBC) isolated from membranes of the model denitrifying soil bacterium Paracoccus denitrificans is the best characterized example of the bacterial respiratory nitric oxide reductases. These are members of the superfamily of heme-copper oxidases and are characterized by the elemental composition of their active site, which contains nonheme iron rather than copper, at which the reductive coupling of two molecules of nitric oxide to form nitrous oxide is catalyzed. This chapter describes methods for the purification and characterization of both native nitric oxide reductase from P. denitrificans and a recombinant form of the enzyme expressed in Escherichia coli, which enables site-directed mutagenesis of the catalytic subunit NorB. Examples are given of electronic absorption and electron paramagnetic resonance spectra that characterize the enzyme in a number of redox states, along with a method for the routine assay of the complex using its natural electron donor pseudoazurin.
- Добавил в систему: Маторин Дмитрий Николаевич
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Полный текст | 2008_-field-Matorin_AD_copy.pdf | 481,8 КБ | 27 февраля 2017 [MatorinDN] |