Electroactive Nanobiomolecular Architectures of Laccase and Cytochrome <i>c</i> on Electrodes: Applying Silica Nanoparticles as Artificial Matrix

Feifel, Sven C.; Kapp, Andreas; Lisdat, Fred

doi:10.1021/la500460n

Cited by 11 publications

(4 citation statements)

References 29 publications

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“…The first assemblies of cyt c with xanthine oxidase still relied on the generation of an internal electron shuttling molecule . However, reaction partners of cyt c such as sulfite oxidase − or laccase , allow the construction of electrode assemblies without the need of any diffusing redox mediator.…”

Section: Technological Applications Of Cytochrome Cmentioning

confidence: 99%

Multifunctional Cytochrome c: Learning New Tricks from an Old Dog

et al. 2017

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Cytochrome c (cyt c) is a small soluble heme protein characterized by a relatively flexible structure, particularly in the ferric form, such that it is able to sample a broad conformational space. Depending on the specific conditions, interactions, and cellular localization, different conformations may be stabilized, which differ in structure, redox properties, binding affinities, and enzymatic activity. The primary function is electron shuttling in oxidative phosphorylation, and is exerted by the so-called native cyt c in the intermembrane mitochondrial space of healthy cells. Under pro-apoptotic conditions, however, cyt c gains cardiolipin peroxidase activity, translocates into the cytosol to engage in the intrinsic apoptotic pathway, and enters the nucleus where it impedes nucleosome assembly. Other reported functions include cytosolic redox sensing and involvement in the mitochondrial oxidative folding machinery. Moreover, post-translational modifications such as nitration, phosphorylation, and sulfoxidation of specific amino acids induce alternative conformations with differential properties, at least in vitro. Similar structural and functional alterations are elicited by biologically significant electric fields and by naturally occurring mutations of human cyt c that, along with mutations at the level of the maturation system, are associated with specific diseases. Here, we summarize current knowledge and recent advances in understanding the different structural, dynamic, and thermodynamic factors that regulate the primary electron transfer function, as well as alternative functions and conformations of cyt c. Finally, we present recent technological applications of this moonlighting protein.

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Section: Technological Applications Of Cytochrome Cmentioning

confidence: 99%

Multifunctional Cytochrome c: Learning New Tricks from an Old Dog

et al. 2017

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“…The key point of this biomacromolecular architecture is the incorporation of the enzyme in a matrix of the electron shuttling redox protein. This is based on the self-exchange capability of cyt c which can be retained even when immobilized by adsorption in multiple layers on electrodes. ,, Cyt c acts consequently not only as a reaction partner of FDH but also as a wiring agent connecting the enzyme molecules with the electrode by repeated interprotein electron transfer steps. Addressing the stabilization of this biprotein construction, the negatively charged DNA was used as a second building block.…”

Section: Results and Discussionmentioning

confidence: 99%

Interaction of Flavin-Dependent Fructose Dehydrogenase with Cytochrome c as Basis for the Construction of Biomacromolecular Architectures on Electrodes

et al. 2016

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The creation of electron transfer (ET) chains based on the defined arrangement of enzymes and redox proteins on electrode surfaces represents an interesting approach within the field of bioelectrocatalysis. In this study, we investigated the ET reaction of the flavin-dependent enzyme fructose dehydrogenase (FDH) with the redox protein cytochrome c (cyt c). Two different pH optima were found for the reaction in acidic and neutral solutions. When cyt c was adsorbed on an electrode surface while the enzyme remained in solution, ET proceeded efficiently in media of neutral pH. Interprotein ET was also observed in acidic media; however, it appeared to be less efficient. These findings suggest that two different ET pathways between the enzyme and cyt c may occur. Moreover, cyt c and FDH were immobilized in multiple layers on an electrode surface by means of another biomacromolecule: DNA (double stranded) using the layer-by-layer technique. The biprotein multilayer architecture showed a catalytic response in dependence on the fructose concentration, indicating that the ET reaction between both proteins is feasible even in the immobilized state. The electrode showed a defined response to fructose and a good storage stability. Our results contribute to the better understanding of the ET reaction between FDH and cyt c and provide the basis for the creation of all-biomolecule based fructose sensors the sensitivity of which can be controlled by the layer preparation.

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“…The authors could show that electrons were first transferred to the heme with the higher potential and then to the second, low-potential heme by fast intramolecular ET. Lisdat and coworkers reported extensive studies on a multilayered protein-enzyme system on SAM-modified gold electrodes [96][97][98][99]. For example, they described a sulfite oxidase/cyt c (SOx/cyt c) multilayer system without polyelectrolyte, repeatedly incubating the prepared cyt c-modified Au electrode into a mixture of SOx/cyt c solution and pure cyt c solution [97].…”

Section: Cytochrome Cmentioning

confidence: 99%

Direct Electrochemical Enzyme Electron Transfer on Electrodes Modified by Self-Assembled Molecular Monolayers

et al. 2020

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Self-assembled molecular monolayers (SAMs) have long been recognized as crucial “bridges” between redox enzymes and solid electrode surfaces, on which the enzymes undergo direct electron transfer (DET)—for example, in enzymatic biofuel cells (EBFCs) and biosensors. SAMs possess a wide range of terminal groups that enable productive enzyme adsorption and fine-tuning in favorable orientations on the electrode. The tunneling distance and SAM chain length, and the contacting terminal SAM groups, are the most significant controlling factors in DET-type bioelectrocatalysis. In particular, SAM-modified nanostructured electrode materials have recently been extensively explored to improve the catalytic activity and stability of redox proteins immobilized on electrochemical surfaces. In this report, we present an overview of recent investigations of electrochemical enzyme DET processes on SAMs with a focus on single-crystal and nanoporous gold electrodes. Specifically, we consider the preparation and characterization methods of SAMs, as well as SAM applications in promoting interfacial electrochemical electron transfer of redox proteins and enzymes. The strategic selection of SAMs to accord with the properties of the core redox protein/enzymes is also highlighted.

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Electroactive Nanobiomolecular Architectures of Laccase and Cytochrome c on Electrodes: Applying Silica Nanoparticles as Artificial Matrix

Cited by 11 publications

References 29 publications

Multifunctional Cytochrome c: Learning New Tricks from an Old Dog

Multifunctional Cytochrome c: Learning New Tricks from an Old Dog

Interaction of Flavin-Dependent Fructose Dehydrogenase with Cytochrome c as Basis for the Construction of Biomacromolecular Architectures on Electrodes

Direct Electrochemical Enzyme Electron Transfer on Electrodes Modified by Self-Assembled Molecular Monolayers

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