Abstract
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 language | English |
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Article number | 8006 |
Pages (from-to) | 1-8 |
Number of pages | 8 |
Journal | Scientific Reports |
Volume | 11 |
Early online date | 13 Apr 2021 |
DOIs | |
Publication status | Published - 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:
Copyright 2021 Elsevier B.V., All rights reserved.
Funding
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.
Funders | Funder number |
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Japan Society for the Promotion of Science | 16K07299 |
Japan Society for the Promotion of Science |