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Nanobiomolecular Multiprotein Clusters on Electrodes for the Formation of a Switchable Cascadic Reaction Scheme
Author(s) -
Feifel Sven C.,
Kapp Andreas,
Ludwig Roland,
Lisdat Fred
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201310437
Subject(s) - cellobiose dehydrogenase , chemistry , redox , electrode , electron transfer , supramolecular chemistry , cytochrome c , analyte , heme , biosensor , combinatorial chemistry , cellobiose , photochemistry , enzyme , inorganic chemistry , organic chemistry , molecule , chromatography , biochemistry , mitochondrion , cellulase
A supramolecular multicomponent protein architecture on electrodes is developed that allows the establishment of bidirectional electron transfer cascades based on interprotein electron exchange. The architecture is formed by embedding two different enzymes (laccase and cellobiose dehydrogenase) and a redox protein (cytochrome c ) by means of carboxy‐modified silica nanoparticles in a multiple layer format. The construct is designed as a switchable dual analyte detection device allowing the measurement of lactose and oxygen, respectively. As the switching force we apply the electrode potential, which ensures control of the redox state of cytochrome c . The two signal chains are operating in a non‐separated matrix and are not disturbed by the other biocatalyst.