title: Engineering of supramolecular photoactive protein architectures: the defined co-assembly of photosystem I and cytochrome c using a nanoscaled DNA-matrix.
abstract: The engineering of renewable and sustainable protein-based light-to-energy converting systems is an emerging field of research. Here, we report on the development of supramolecular light-harvesting electrodes, consisting of the redox protein cytochrome c working as a molecular scaffold as well as a conductive wiring network and photosystem I as a photo-functional matrix element. Both proteins form complexes in solution, which in turn can be adsorbed on thiol-modified gold electrodes through a self-assembly mechanism. To overcome the limited stability of self-grown assemblies, DNA, a natural polyelectrolyte, is used as a further building block for the construction of a photo-active 3D architecture. DNA acts as a structural matrix element holding larger protein amounts and thus remarkably improving the maximum photocurrent and electrode stability. On investigating the photophysical properties, this system demonstrates that effective electron pathways have been created.
authors.affiliation: Technical University of Applied Sciences Wildau, Institute of Applied Life Sciences, Biosystems Technology, Hochschulring 1, 15745 Wildau, Germany. flisdat@th-wildau.de.
authors.forename: Kai R
authors.initials: KR
authors.lastname: Stieger
authors.affiliation: Technical University of Applied Sciences Wildau, Institute of Applied Life Sciences, Biosystems Technology, Hochschulring 1, 15745 Wildau, Germany. flisdat@th-wildau.de.
authors.forename: Dmitri
authors.initials: D
authors.lastname: Ciornii
authors.affiliation: Humboldt-University of Berlin, Institute of Biology, Biochemistry and Structural Biology, Unter den Linden 6, 10099 Berlin, Germany.
authors.forename: Adrian
authors.initials: A
authors.lastname: Kölsch
authors.affiliation: Humboldt-University of Berlin, Institute of Biology, Biochemistry and Structural Biology, Unter den Linden 6, 10099 Berlin, Germany.
authors.forename: Mahdi
authors.initials: M
authors.lastname: Hejazi
authors.affiliation: University of Glasgow, Glasgow Biomedical Research Centre, Institute for Molecular, Cell & Systems Biology, 120 University Place, Glasgow, G12 8TA, Scotland, UK.
authors.forename: Heiko
authors.initials: H
authors.lastname: Lokstein
authors.affiliation: Technical University of Applied Sciences Wildau, Institute of Applied Life Sciences, Biosystems Technology, Hochschulring 1, 15745 Wildau, Germany. flisdat@th-wildau.de.
authors.forename: Sven C
authors.initials: SC
authors.lastname: Feifel
authors.affiliation: Humboldt-University of Berlin, Institute of Biology, Biochemistry and Structural Biology, Unter den Linden 6, 10099 Berlin, Germany.
authors.forename: Athina
authors.initials: A
authors.lastname: Zouni
authors.affiliation: Technical University of Applied Sciences Wildau, Institute of Applied Life Sciences, Biosystems Technology, Hochschulring 1, 15745 Wildau, Germany. flisdat@th-wildau.de.
authors.forename: Fred
authors.initials: F
authors.lastname: Lisdat
mesh_terms: D000458:Cyanobacteria / Q000201:enzymology; D045304:Cytochromes c / Q000737:chemistry*; D004247:DNA / Q000737:chemistry*; D004566:Electrodes; D010084:Oxidation-Reduction; D045331:Photosystem I Protein Complex / Q000737:chemistry*; D015202:Protein Engineering
chemical_list: D045331:Photosystem I Protein Complex; D045304:Cytochromes c; D004247:DNA