Cytochrome bd Displays Significant Quinol Peroxidase Activity

Al-Attar, S.; Yu, Y.; Pinkse, M.W.H.; Hoeser, Jo; Friedrich, Thorsten; Bald, Dirk; de Vries, S.

doi:10.1038/srep27631

Cytochrome bd Displays Significant Quinol Peroxidase Activity

Title

Cytochrome bd Displays Significant Quinol Peroxidase Activity

Author

Al-Attar, S. (TU Delft BT/Biocatalysis)
Yu, Y. (TU Delft OLD BT/Analytical Biotechnology)
Pinkse, M.W.H. (TU Delft OLD BT/Analytical Biotechnology)
Hoeser, Jo (Albert-Ludwigs-Universität Freiburg)
Friedrich, Thorsten (Albert-Ludwigs-Universität Freiburg)
Bald, Dirk (Vrije Universiteit Amsterdam)
de Vries, S. (TU Delft BT/Biocatalysis)

Date

2016-06-09

Abstract

Cytochrome bd is a prokaryotic terminal oxidase that catalyses the electrogenic reduction of oxygen to water using ubiquinol as electron donor. Cytochrome bd is a tri-haem integral membrane enzyme carrying a low-spin haem b₅₅₈, and two high-spin haems: b₅₉₅ and d. Here we show that besides its oxidase activity, cytochrome bd from Escherichia coli is a genuine quinol peroxidase (QPO) that reduces hydrogen peroxide to water. The highly active and pure enzyme preparation used in this study did not display the catalase activity recently reported for E. coli cytochrome bd. To our knowledge, cytochrome bd is the first membrane-bound quinol peroxidase detected in E. coli. The observation that cytochrome bd is a quinol peroxidase, can provide a biochemical basis for its role in detoxification of hydrogen peroxide and may explain the frequent findings reported in the literature that indicate increased sensitivity to hydrogen peroxide and decreased virulence in mutants that lack the enzyme.

Subject

Bacterial pathogenesis
Oxidoreductases

To reference this document use:

http://resolver.tudelft.nl/uuid:358f2682-c0c2-45aa-998f-92e9b6b7b4b4

DOI

https://doi.org/10.1038/srep27631

ISSN

2045-2322

Source

Scientific Reports, 6

Part of collection

Institutional Repository