Non-covalent functionalization of multi-walled carbon nanotubes with cytochrome c: Enhanced direct electron transfer and analytical applications

Eguílaz, Marcos; Gutiérrez, Alejandro García; Rivas, Gustavo A.

doi:10.1016/j.snb.2015.11.011

Cited by 49 publications

(19 citation statements)

References 48 publications

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“…The device had a low sensitivity (0.0178 A M −1 cm −2 ) in a broad linear range (Table 1) [128]. In the absence of polymers, the sensitivity was increased up to 0.043 A M -1 cm −2 [245]. However, in this case, the interaction of cyt c with the immobilization components induced a red-shift of the Soret band and a lower formal potential (−0.128 V), which indicated the presence of a non-native state [245].…”

Section: Cytochrome C and Microperoxidasesmentioning

confidence: 99%

Electrocatalysis by Heme Enzymes—Applications in Biosensing

et al. 2021

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Heme proteins take part in a number of fundamental biological processes, including oxygen transport and storage, electron transfer, catalysis and signal transduction. The redox chemistry of the heme iron and the biochemical diversity of heme proteins have led to the development of a plethora of biotechnological applications. This work focuses on biosensing devices based on heme proteins, in which they are electronically coupled to an electrode and their activity is determined through the measurement of catalytic currents in the presence of substrate, i.e., the target analyte of the biosensor. After an overview of the main concepts of amperometric biosensors, we address transduction schemes, protein immobilization strategies, and the performance of devices that explore reactions of heme biocatalysts, including peroxidase, cytochrome P450, catalase, nitrite reductase, cytochrome c oxidase, cytochrome c and derived microperoxidases, hemoglobin, and myoglobin. We further discuss how structural information about immobilized heme proteins can lead to rational design of biosensing devices, ensuring insights into their efficiency and long-term stability.

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Section: Cytochrome C and Microperoxidasesmentioning

confidence: 99%

Electrocatalysis by Heme Enzymes—Applications in Biosensing

et al. 2021

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“…It is known that Cyt c adsorbs strongly on conventional metal electrodes like Pt, Hg, Au or Ag 17 and conformational changes suffered by the protein (unfolding and/or denaturation) lead to slow electrontransfer kinetics 18,19 . This difficulty has been overcome by using electrode modifiers such as metal oxides, advanced carbon materials, DNA or lipid membranes [20][21][22][23][24][25][26] . In particular, the modification of surfaces with organic thin films like self-assembled monolayers (SAM), has been extensively used to manipulate the electrode surface, promoting the appropriate orientation of the protein and thus enhancing its electroactivity [27][28][29][30][31][32][33][34][35][36] .…”

Section: Introductionmentioning

confidence: 99%

Direct Electron Transfer to Cytochrome c Induced by a Conducting Polymer

et al. 2017

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The direct electron transfer (DET) to redox proteins has become a central topic in the development of biotechnological devices. The present work explores the mechanisms of the direct electrochemistry between cytochrome c and a conducting polymer, PEDOT-PSS. This polymer has been electrosynthesized from its monomers in aqueous solution on gold electrodes and its capabilities for DET to cyt c have been examined by electrochemical and spectroelectrochemical methods. The polymer was electrodeposited with controlled thickness and we determined the electron transfer rate constant for cyt c oxidation was about 2 orders of magnitude higher than those obtained at conventional electrodes. Spectroelectrochemical measurements allowed to evaluate the redox state of the polymer as a function of the potential and, in addition, the observation of intrinsic cyt c redox activity upon electron transfer from the conducting polymer. During the oxidation process of this protein, lysine residues placed near the heme crevice interact electrostatically with the anionic polyelectrolyte PSS. This interaction favors the orientation of the heme group towards the chains of PEDOT backbone, which is the eventual responsible for the electron transfer to the protein.3

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“…Other materials, such as graphene oxide [ 136 , 137 , 138 ], carbon nanotubes [ 139 , 140 ], ZrO 2 [ 141 ], Ni foam [ 142 ], ZnO [ 143 ], and TiO 2 [ 144 ], have also provided promising results. For example, as shown in Figure 9 a, Zhao et al [ 145 ] integrated Cyt-c with AuNPs on 3D graphene aerogel to remedy the effect of poor DET, and Lee et al [ 146 ] employed a combination of graphene oxide as a conductive material with Cyt-c for the detection of H 2 O 2 ( Figure 9 b).…”

Section: Hydrogen Peroxide (H 2 O 2 mentioning

confidence: 99%

Detection Technologies for Reactive Oxygen Species: Fluorescence and Electrochemical Methods and Their Applications

et al. 2021

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Reactive oxygen species (ROS) have been found in plants, mammals, and natural environmental processes. The presence of ROS in mammals has been linked to the development of severe diseases, such as diabetes, cancer, tumors, and several neurodegenerative conditions. The most common ROS involved in human health are superoxide (O2•−), hydrogen peroxide (H2O2), and hydroxyl radicals (•OH). Organic and inorganic molecules have been integrated with various methods to detect and monitor ROS for understanding the effect of their presence and concentration on diseases caused by oxidative stress. Among several techniques, fluorescence and electrochemical methods have been recently developed and employed for the detection of ROS. This literature review intends to critically discuss the development of these techniques to date, as well as their application for in vitro and in vivo ROS detection regarding free-radical-related diseases. Moreover, important insights into and further steps for using fluorescence and electrochemical methods in the detection of ROS are presented.

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Non-covalent functionalization of multi-walled carbon nanotubes with cytochrome c: Enhanced direct electron transfer and analytical applications

Cited by 49 publications

References 48 publications

Electrocatalysis by Heme Enzymes—Applications in Biosensing

Electrocatalysis by Heme Enzymes—Applications in Biosensing

Direct Electron Transfer to Cytochrome c Induced by a Conducting Polymer

Detection Technologies for Reactive Oxygen Species: Fluorescence and Electrochemical Methods and Their Applications

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