Nanobiomolecular Multiprotein Clusters on Electrodes for the Formation of a Switchable Cascadic Reaction Scheme

Abstract

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.

Inter‐domain electron transfer in cellobiose dehydrogenase: modulation by pH and divalent cations

“…for increasing the current output of CDH‐based biosensors or biofuel cells. Also, in accordance with the results of a previous study , a CDH‐based bioelectrochemical switch may be accomplished at neutral/alkaline pH using divalent cations to switch the IET and hence direct electron transfer on and off. The high millimolar dication concentrations required for such an effect are rarely encountered in nature, but may provide ways to stabilize or regulate enzymes in biocatalytic and biomedical applications.…”

Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics

“…In an inspiring study, Lisdat and coworkers designed a multicomponent protein system on the electrode surface consisting of laccase, cellobiose dehydrogenase, and cytochrome c embedded in carboxy-modified nanoparticles. The electrode force controls the redox state of cytochrome c and was used to switch between two different ET cascade reactions for the detection of O 2 or lactose (Figure 10) [140]. …”

“…Reprinted with permission from Ref. [140]. Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim under license number 3636620458132.…”

Interprotein Electron Transfer between FeS‐Protein Nanowires and Oxygen‐Tolerant NiFe Hydrogenase

“…[1][2][3][4][5][6][7][8] Ad irect electron transfer (DET) between the enzymes and electrodes is possible and can be effective for functional biofuel cells. These processes involve chains of redox proteins and long-range electron transport between enzymes.T he efficiency and specificity of these phenomena have driven research interest in biomimetic conductive biomaterials,m aking them very tempting for the design of biosensors and electrocatalytic devices.T he confinement on the electrode surface of small electron carrier proteins together with enzymes within organized films are required for efficient inter-protein electron transfers and electrical communication with the electrode.…”

“…These processes involve chains of redox proteins and long-range electron transport between enzymes.T he efficiency and specificity of these phenomena have driven research interest in biomimetic conductive biomaterials,m aking them very tempting for the design of biosensors and electrocatalytic devices.T he confinement on the electrode surface of small electron carrier proteins together with enzymes within organized films are required for efficient inter-protein electron transfers and electrical communication with the electrode. [1][2][3][4][5][6][7][8] Ad irect electron transfer (DET) between the enzymes and electrodes is possible and can be effective for functional biofuel cells. [9][10][11] Mediated electron transfer (MET) employs redox polymers to immobilize enzymes and shuttle electrons to the active site.This type of MET approach exhibits important advantages over DET: an immobilization matrix for enzymes,a ni ncrease of the number of wired enzymes within the 3D matrix, and provides aprotecting layer for preventing enzyme denaturation or deactivation.…”