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

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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 K _M 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 bo ₃ from E. coli. Taken together, CL can enhance the activity of detergent-solubilized cytochrome bd and cytochrome bo ₃.

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The cytochrome bd respiratory oxygen reductases.

Vitaliy B. Borisov, Robert B Gennis, James Hemp … (2011)

Cytochrome bd is a respiratory quinol: O₂ oxidoreductase found in many prokaryotes, including a number of pathogens. The main bioenergetic function of the enzyme is the production of a proton motive force by the vectorial charge transfer of protons. The sequences of cytochromes bd are not homologous to those of the other respiratory oxygen reductases, i.e., the heme-copper oxygen reductases or alternative oxidases (AOX). Generally, cytochromes bd are noteworthy for their high affinity for O₂ and resistance to inhibition by cyanide. In E. coli, for example, cytochrome bd (specifically, cytochrome bd-I) is expressed under O₂-limited conditions. Among the members of the bd-family are the so-called cyanide-insensitive quinol oxidases (CIO) which often have a low content of the eponymous heme d but, instead, have heme b in place of heme d in at least a majority of the enzyme population. However, at this point, no sequence motif has been identified to distinguish cytochrome bd (with a stoichiometric complement of heme d) from an enzyme designated as CIO. Members of the bd-family can be subdivided into those which contain either a long or a short hydrophilic connection between transmembrane helices 6 and 7 in subunit I, designated as the Q-loop. However, it is not clear whether there is a functional consequence of this difference. This review summarizes current knowledge on the physiological functions, genetics, structural and catalytic properties of cytochromes bd. Included in this review are descriptions of the intermediates of the catalytic cycle, the proposed site for the reduction of O₂, evidence for a proton channel connecting this active site to the bacterial cytoplasm, and the molecular mechanism by which a membrane potential is generated. 2011 Elsevier B.V. All rights reserved.

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Architecture of succinate dehydrogenase and reactive oxygen species generation.

Victoria Yankovskaya, Rob Horsefield, Susanna Törnroth … (2003)

The structure of Escherichia coli succinate dehydrogenase (SQR), analogous to the mitochondrial respiratory complex II, has been determined, revealing the electron transport pathway from the electron donor, succinate, to the terminal electron acceptor, ubiquinone. It was found that the SQR redox centers are arranged in a manner that aids the prevention of reactive oxygen species (ROS) formation at the flavin adenine dinucleotide. This is likely to be the main reason SQR is expressed during aerobic respiration rather than the related enzyme fumarate reductase, which produces high levels of ROS. Furthermore, symptoms of genetic disorders associated with mitochondrial SQR mutations may be a result of ROS formation resulting from impaired electron transport in the enzyme.

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Membrane proteins bind lipids selectively to modulate their structure and function

Arthur Laganowsky, Eamonn Reading, Timothy Allison … (2014)

Previous studies have established that the folding, structure and function of membrane proteins are influenced by their lipid environments 1-7 and that lipids can bind to specific sites, for example in potassium channels 8 . Fundamental questions remain however regarding the extent of membrane protein selectivity toward lipids. Here we report a mass spectrometry (MS) approach designed to determine the selectivity of lipid binding to membrane protein complexes. We investigate the mechanosensitive channel of large conductance (MscL), aquaporin Z (AqpZ), and the ammonia channel (AmtB) using ion mobility MS (IM-MS), which reports gas-phase collision cross sections. We demonstrate that folded conformations of membrane protein complexes can exist in the gas-phase. By resolving lipid-bound states we then rank bound lipids based on their ability to resist gas phase unfolding and thereby stabilize membrane protein structure. Results show that lipids bind non-selectively and with high avidity to MscL, all imparting comparable stability, the highest-ranking lipid however is phosphatidylinositol phosphate, in line with its proposed functional role in mechanosensation 9 . AqpZ is also stabilized by many lipids with cardiolipin imparting the most significant resistance to unfolding. Subsequently, through functional assays, we discover that cardiolipin modulates AqpZ function. Analogous experiments identify AmtB as being highly selective for phosphatidylglycerol prompting us to obtain an X-ray structure in this lipid membrane-like environment. The 2.3Å resolution structure, when compared with others obtained without lipid bound, reveals distinct conformational changes that reposition AmtB residues to interact with the lipid bilayer. Overall our results demonstrate that resistance to unfolding correlates with specific lipid-binding events enabling distinction of lipids that merely bind from those that modulate membrane protein structure and/or function. We anticipate that these findings will be influential not only for defining the selectivity of membrane proteins toward lipids but also for understanding the role of lipids in modulating function or drug binding.

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Author and article information

Contributors

Duncan G. G. McMillan: D.G.G.McMillan@tudelft.nl

Dirk Bald: d.bald@vu.nl

Journal

Journal ID (nlm-ta): Sci Rep

Journal ID (iso-abbrev): Sci Rep

Title: Scientific Reports

Publisher: Nature Publishing Group UK (London )

ISSN (Electronic): 2045-2322

Publication date (Electronic): 13 April 2021

Publication date PMC-release: 13 April 2021

Publication date Collection: 2021

Volume: 11

Electronic Location Identifier: 8006

Affiliations

[1 ]GRID grid.12380.38, ISNI 0000 0004 1754 9227, Department of Molecular Cell Biology, Amsterdam Institute of Molecular and Life Sciences (AIMMS), Faculty of Science, , Vrije Universiteit Amsterdam, ; De Boelelaan 1108, 1081 HZ Amsterdam, The Netherlands

[2 ]GRID grid.412125.1, ISNI 0000 0001 0619 1117, Department of Biochemistry, Faculty of Science, , King Abdulaziz University, ; Jeddah, 21589 Saudi Arabia

[3 ]GRID grid.5292.c, ISNI 0000 0001 2097 4740, Department of Biotechnology, , Delft University of Technology, ; Van der Maasweg 9, 2629 HZ Delft, The Netherlands

[4 ]GRID grid.258806.1, ISNI 0000 0001 2110 1386, Department of Bioscience and Bioinformatics, , Kyushu Institute of Technology, ; Kawazu 680-4, Iizuka, Fukuoka-ken 820-8502 Japan

Article

Publisher ID: 87354

DOI: 10.1038/s41598-021-87354-0

PMC ID: 8044227

SO-VID: fe7a310f-cff7-467c-8b9c-254ca1dd212d

License:

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

History

Date received : 16 July 2020

Date accepted : 25 March 2021

Funding

Funded by: Japan Society for the Promotion of Science

Award ID: Grant-in-Aid for Scientific Research (C) (16K07299)

Award Recipient : Junshi Sakamoto

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ScienceOpen disciplines: Uncategorized

Keywords: enzymes,chemical biology

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ScienceOpen disciplines: Uncategorized

Keywords: enzymes, chemical biology

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

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Most cited references 50

The cytochrome bd respiratory oxygen reductases.

Architecture of succinate dehydrogenase and reactive oxygen species generation.

Membrane proteins bind lipids selectively to modulate their structure and function

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