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Effect of lipid bilayer properties on the photocycle of green proteorhodopsin
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 8
2015 (English)In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1847, no 8, 698-708 p.Article in journal (Refereed) Published
Abstract [en]

The significance of specific lipids for proton pumping by the bacterial rhodopsin proteorhodopsin (pR) was studied. To this end, it was examined whether pR preferentially binds certain lipids and whether molecular properties of the lipid environment affect the photocycle. pR's photocyde was followed by microsecond flash-photolysis in the visible spectral range. It was fastest in phosphatidylcholine liposomes (soy bean lipid), intermediate in 3-[(3-cholamidopropyl) dimethylammonio] propanesulfonate (CHAPS): 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) bicelles and in Triton X-100, and slowest when pR was solubilized in CHAPS. In bicelles with different lipid compositions, the nature of the head groups, the unsaturation level and the fatty acid chain length had small effects on the photocycle. The specific affinity of pR for lipids of the expression host Eschetichia coil was investigated by an optimized method of lipid isolation from purified membrane protein using two different concentrations of the detergent N-dodecyl-beta-D-maltoside (DDM). We found that 11 lipids were copurified per pR molecule at 0.1% DDM, whereas essentially all lipids were stripped off from pR by 1% DDM. The relative amounts of copurifled phosphatidylethanolamine, phosphatidylglycerol, and cardiolipin did not correlate with the molar percentages normally present in E. coil cells. The results indicate a predominance of phosphatidylethanolamine species in the lipid annulus around recombinant pR that are less polar than the dominant species in the cell membrane of the expression host E. coli.

Place, publisher, year, edition, pages
2015. Vol. 1847, no 8, 698-708 p.
Keyword [en]
Proteorhodopsin, Bicelle, Lipid, Detergent, Membrane protein, Photocycle
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-119116DOI: 10.1016/j.bbabio.2015.04.011ISI: 000356547100003OAI: oai:DiVA.org:su-119116DiVA: diva2:843836
Available from: 2015-07-31 Created: 2015-07-29 Last updated: 2017-12-04Bibliographically approved

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Ariöz, CandanLiebau, JobstMäler, Lenavon Ballmoos, ChristophBarth, Andreas
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