Insights into Interprotein Electron Transfer of Human Cytochrome c Variants Arranged in Multilayer Architectures by Means of an Artificial Silica Nanoparticle Matrix

ACS Omega
Sven C FeifelFred Lisdat

Abstract

The redox behavior of proteins plays a crucial part in the design of bioelectronic systems. We have demonstrated several functional systems exploiting the electron exchange properties of the redox protein cytochrome c (cyt c) in combination with enzymes and photoactive proteins. The operation is based on an effective reaction at modified electrodes but also to a large extent on the capability of self-exchange between cyt c molecules in a surface-fixed state. In this context, different variants of human cyt c have been examined here with respect to an altered heterogeneous electron transfer (ET) rate in a monolayer on electrodes as well as an enhanced self-exchange rate while being incorporated in multilayer architectures. For this purpose, mutants of the wild-type (WT) protein have been prepared to change the chemical nature of the surface contact area near the heme edge. The structural integrity of the variants has been verified by NMR and UV-vis measurements. It is shown that the single-point mutations can significantly influence the heterogeneous ET rate at thiol-modified gold electrodes and that electroactive protein/silica nanoparticle multilayers can be constructed with all forms of human cyt c prepared. The kinetic behav...Continue Reading

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Citations

Nov 2, 2017·Journal of the American Chemical Society·Dmitri CiorniiFred Lisdat
Nov 6, 2021·Science Advances·Alonso Gamero-QuijanoMicheál D Scanlon

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Methods Mentioned

BETA
biosensors
amino acid exchange
electron exchange
surface
NMR
quartz crystal microbalance
electrophoresis
chip

Software Mentioned

CHI
PyMOL

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