{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Marusic N"],"funding":["Bundesministerium für Bildung und Forschung","Deutsche Forschungsgemeinschaft","Max-Planck-Gesellschaft"],"pagination":["15006-15017"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7334566"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["117(26)"],"pubmed_abstract":["Cytochrome <i>bo</i> <sub><i>3</i></sub> ubiquinol oxidase is a transmembrane protein, which oxidizes ubiquinone and reduces oxygen, while pumping protons. Apart from its combination with F<sub>1</sub>F<sub>o</sub>-ATPase to assemble a minimal ATP regeneration module, the utility of the proton pump can be extended to other applications in the context of synthetic cells such as transport, signaling, and control of enzymatic reactions. In parallel, polymers have been speculated to be phospholipid mimics with respect to their ability to self-assemble in compartments with increased stability. However, their usability as interfaces for complex membrane proteins has remained questionable. In the present work, we optimized a fusion/electroformation approach to reconstitute <i>bo</i> <sub><i>3</i>"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Constructing artificial respiratory chain in polymer compartments: Insights into the interplay between <i>bo</i> <sub><i>3</i></sub> oxidase and the membrane."],"pmcid":["PMC7334566"],"funding_grant_id":["MaxSynBio","391498659"],"pubmed_authors":["Vidakovic-Koch T","Sundmacher K","Dimova R","Ivanov I","Otrin L","Hamdi F","Kastritis PL","Zhao Z","Lira RB","Kyrilis FL","Marusic N"],"additional_accession":[]},"is_claimable":false,"name":"Constructing artificial respiratory chain in polymer compartments: Insights into the interplay between <i>bo</i> <sub><i>3</i></sub> oxidase and the membrane.","description":"Cytochrome <i>bo</i> <sub><i>3</i></sub> ubiquinol oxidase is a transmembrane protein, which oxidizes ubiquinone and reduces oxygen, while pumping protons. Apart from its combination with F<sub>1</sub>F<sub>o</sub>-ATPase to assemble a minimal ATP regeneration module, the utility of the proton pump can be extended to other applications in the context of synthetic cells such as transport, signaling, and control of enzymatic reactions. In parallel, polymers have been speculated to be phospholipid mimics with respect to their ability to self-assemble in compartments with increased stability. However, their usability as interfaces for complex membrane proteins has remained questionable. In the present work, we optimized a fusion/electroformation approach to reconstitute <i>bo</i> <sub><i>3</i>","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Jun","modification":"2025-06-01T01:48:47.764Z","creation":"2025-06-01T01:48:47.764Z"},"accession":"S-EPMC7334566","cross_references":{"pubmed":["32554497"],"doi":["10.1073/pnas.1919306117"]}}