Please use this identifier to cite or link to this item: http://dx.doi.org/10.14279/depositonce-5991
Main Title: Multilayered lipid membrane stacks for biocatalysis using membrane enzymes
Author(s): Heath, George R.
Li, Mengqiu
Rong, Honling
Radu, Valentin
Frielingsdorf, Stefan
Lenz, Oliver
Butt, Julea N.
Jeuken, Lars J. C.
Type: Article
Language Code: en
Abstract: Multilayered or stacked lipid membranes are a common principle in biology and have various functional advantages compared to single-lipid membranes, such as their ability to spatially organize processes, compartmentalize molecules, and greatly increase surface area and hence membrane protein concentration. Here, a supramolecular assembly of a multilayered lipid membrane system is reported in which poly-l-lysine electrostatically links negatively charged lipid membranes. When suitable membrane enzymes are incorporated, either an ubiquinol oxidase (cytochrome bo(3) from Escherichia coli) or an oxygen tolerant hydrogenase (the membrane-bound hydrogenase from Ralstonia eutropha), cyclic voltammetry (CV) reveals a linear increase in bio-catalytic activity with each additional membrane layer. Electron transfer between the enzymes and the electrode is mediated by the quinone pool that is present in the lipid phase. Using atomic force microscopy, CV, and fluorescence microscopy it is deduced that quinones are able to diffuse between the stacked lipid membrane layers via defect sites where the lipid membranes are inter-connected. This assembly is akin to that of interconnected thylakoid membranes or the folded lamella of mitochondria and has significant potential for mimicry in biotechnology applications such as energy production or biosensing.
URI: http://depositonce.tu-berlin.de/handle/11303/6483
http://dx.doi.org/10.14279/depositonce-5991
Issue Date: 2017
Date Available: 14-Jul-2017
DDC Class: 620 Ingenieurwissenschaften und Maschinenbau ; 540 Chemie ; 530 Physik
Subject(s): biocatalysis
biomimicry
layer-by-layer assembly
self-assembly
solid supported membranes
Sponsor/Funder: EC/FP7/280518/EU/Membrane-modified Electrodes to study Membrane Enzymes/MEME
DFG, EXC 314, Unifying Concepts in Catalysis
Creative Commons License: https://creativecommons.org/licenses/by/4.0/
Journal Title: Advanced Functional Materials
Publisher: Wiley-VCH
Publisher Place: Weinheim
Volume: 27
Issue: 17
Article Number: 1606265
Publisher DOI: 10.1002/adfm.201606265
EISSN: 1616-3028
ISSN: 1616-301X
Appears in Collections:Technische Universität Berlin » Fakultäten & Zentralinstitute » Fakultät 2 Mathematik und Naturwissenschaften » Institut für Chemie » Fachgebiet Physikalische Chemie / Biophysikalische Chemie » Publications

Files in This Item:
File Description SizeFormat 
10.1002.adfm.201606265.pdf3.31 MBAdobe PDFThumbnail
View/Open


Items in DepositOnce are protected by copyright, with all rights reserved, unless otherwise indicated.