Cardiolipin enhances the enzymatic activity of cytochrome bd and cytochrome bo 3 solubilized in dodecyl-maltoside

Amer H. Asseri, Albert Godoy-Hernandez, Hojjat Ghasemi Goojani, Holger Lill, Junshi Sakamoto, Duncan G.G. McMillan, Dirk Bald*

*Corresponding author for this work

Research output: Contribution to JournalArticleAcademicpeer-review


Cardiolipin (CL) is a lipid that is found in the membranes of bacteria and the inner membranes of mitochondria. CL can increase the activity of integral membrane proteins, in particular components of respiratory pathways. We here report that CL activated detergent-solubilized cytochrome bd, a terminal oxidase from Escherichia coli. CL enhanced the oxygen consumption activity ~ twofold and decreased the apparent KM value for ubiquinol-1 as substrate from 95 µM to 35 µM. Activation by CL was also observed for cytochrome bd from two Gram-positive species, Geobacillus thermodenitrificans and Corynebacterium glutamicum, and for cytochrome bo3 from E. coli. Taken together, CL can enhance the activity of detergent-solubilized cytochrome bd and cytochrome bo3.

Original languageEnglish
Article number8006
Pages (from-to)1-8
Number of pages8
JournalScientific Reports
Early online date13 Apr 2021
Publication statusPublished - Dec 2021

Bibliographical note

Funding Information:
This work was partly supported by a Grant-in-Aid for Scientific Research (C) (16K07299 to J.S.) from the Japan Society for the Promotion of Science.

Publisher Copyright:
© 2021, The Author(s).

Copyright 2021 Elsevier B.V., All rights reserved.


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