Gold nanoparticles/4-aminothiophenol interfaces for direct electron transfer of horseradish peroxidase: Enzymatic orientation and modulation of sensitivity towards hydrogen peroxide detection

Huerta-Miranda, G.A.; Arrocha-Arcos, A.A.; Miranda-Hernández, M.

doi:10.1016/j.bioelechem.2018.03.004

Cited by 14 publications

(14 citation statements)

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“…The catalytic currents are typically measured by amperometric methods at working potentials between +0.15 and +0.5 V [37,92,93], owing to the high reduction potentials of the catalytic redox couples Fe(III)/compound I and compound I/compound II (e.g., HRP-C E 0' CI/CII +0.898 V) [51,87]. It is noteworthy that cathodic currents are often observed at much lower potentials, consistent with the Fe(III)/Fe(II) redox transition (e.g., −0.35 V for HRP immobilized on modified GC electrodes [94]). In this case, it is likely that the H 2 O 2 detection follows an alternative non-native route, which proceeds via formation of the ferrous [Fe(II)] enzyme.…”

Section: Detection Modes In Peroxidase-based Biosensorsmentioning

confidence: 96%

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: Detection Modes In Peroxidase-based Biosensorsmentioning

confidence: 96%

Electrocatalysis by Heme Enzymes—Applications in Biosensing

et al. 2021

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“…In our group, we have established the conditions to improve the electrochemical response of horseradish peroxidase (HRP) coupled to gold nanoparticles modified with the aromatic alkanothiol 4-aminotiophenol, using glassy carbon (GC) as current collector [24]. We proposed that a critical factor in HRP bioelectrochemical response is to promote conformational changes and proper enzyme orientation when coupled to the electrode.…”

Section: Covalent Immobilization Through Alkanethiol Linkersmentioning

confidence: 99%

“…The nanostructures were modeled as reported elsewhere [54]. Six gold nanoclusters (6 AuNCs) were placed as a thin layer, emulating our previous experimental system (~ 20 nm gold nanoparticles) [24].…”

Section: Building Of Nanomaterials Structuresmentioning

confidence: 99%

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Design of Bioelectrochemical Interfaces Assisted by Molecular Dynamics Simulations

Vidal-Limón¹,

Huerta-Miranda²,

García-García³

et al. 2021

Homology Molecular Modeling - Perspectives and Applications

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The design of bioelectrochemical interfaces (BEI) is an interesting topic that recently demands attention. The synergy between biomolecules and chemical components is necessary to achieve high molecular selectivity and sensitivity for the development of biosensors, synthesis of different compounds, or catalytic processes. For most BEI, the charge transfer process occurs in environments with particular chemical conditions; modeling these environments is a challenging task and requires multidisciplinary efforts. These interfaces can be composed of biomolecules, such as proteins, DNA, or more complex systems like microorganisms. Oxidoreductases enzymes are good candidates, among others, due to their catalytic activities and structural characteristics. In BEI, enzymes are immobilized on conductive surfaces to improve charge transfer processes. Covalent immobilization is the most common method to prolong lifetime or modulate the detection process. However, it is necessary to implement new methodologies that allow the selection of the best candidates for a more efficient design. Homology modeling of oxidoreductases combined with Molecular Dynamics (MD) simulation methods are alternative and already routinely used tools to investigate the structure, dynamics, and thermodynamics of biological molecules. Our motivation is to show different techniques of molecular modeling (Homology Modeling, Gaussian accelerated molecular dynamics, directed adaptive molecular dynamics and electrostatic surface calculations), and using horseradish peroxidase as a model to understand the interactions between biomolecules and gold nanoclusters (as current collector). Additionally, we present our previous studies considering molecular simulations and we discuss recent advances in biomolecular simulations aimed at biosensor design.

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“…It is well-established that the difference in the electrocatalytic behaviour of redox enzymes is driven by their orientation distribution patterns. A random distribution of enzyme orientation commonly leads to low electrocatalytic signal 36 whereas the immobilization of proteins at highly oriented active ET configurations produces excellent bioelectronic yields. 37 Rudiger et al have proved that both orientation and electrocatalytic properties of enzymes bearing a dipole moment can be controlled by electrostatic interactions at the protein/amino-terminated monolayer interfaces.…”

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confidence: 99%