Microperoxidase-11 modified mesoporous SnO<sub>2</sub> film electrodes for the detection of antimalarial drug artemisinin

Ioannidis, Lambros Aris; Nikolaou, Pavlos; Panagiotopoulos, Apostolos; Vassi, Andriana; Topoglidis, Emmanuel

doi:10.1039/c9ay00764d

Cited by 9 publications

(4 citation statements)

References 39 publications

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“…The latter device also showed an extended linear range of 0.4 to 1725 µM [132]. Recently, a MP11-based biosensor was developed for detection of the antimalaria drug artemisinin [257]. The protein was adsorbed onto DDAB and further entrapped into mesoporous SnO 2 NPs.…”

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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“…Additionally, microperoxidase/semiconductor systems have also been used for the electrochemical detection of other compounds than hydrogen peroxide, including glucose via combination with glucose oxidase [144] or nitric oxide [145]. Recently, Ioannidis et al presented an approach for the detection of the antimalarial drug artemisinin where MP-11 was adsorbed to a film of surfactant-modified mesoporous SnO 2 on ITO [146]. Ferrous MP-11 catalyzes the cleavage of an organic peroxide within the artemisinin molecule, which leads to heme re-oxidation, thus invoking an enhanced electrocatalytic reduction current proportional to the concentration of the drug in solution (Figure 7).…”

Section: Heme-peptide Complexesmentioning

confidence: 99%

“…( b ) DPVs of the sensor after the addition of increasing ART concentrations in 10 mM NaH 2 PO 4 pH 7 buffer at a scan rate 0.1 V s −1 . Reprinted from Ioannidis et al, 2019 [ 146 ]. Published by the Royal Society of Chemistry.…”

Section: Figurementioning

confidence: 99%

Electrochemical Biosensors Employing Natural and Artificial Heme Peroxidases on Semiconductors

Neumann

Wollenberger

2020

Sensors

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Heme peroxidases are widely used as biological recognition elements in electrochemical biosensors for hydrogen peroxide and phenolic compounds. Various nature-derived and fully synthetic heme peroxidase mimics have been designed and their potential for replacing the natural enzymes in biosensors has been investigated. The use of semiconducting materials as transducers can thereby offer new opportunities with respect to catalyst immobilization, reaction stimulation, or read-out. This review focuses on approaches for the construction of electrochemical biosensors employing natural heme peroxidases as well as various mimics immobilized on semiconducting electrode surfaces. It will outline important advances made so far as well as the novel applications resulting thereof.

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“…The relatively large irregular charging currents measured with optically transparent SnO 2 electrodes, e.g. [27], prevented confident analysis of the peaks describing redox transformation of adsorbed PioA. However, clear well-defined peaks (figure 4(B)) defining PioA redox activity were measured during cyclic voltammetry of the protein adsorbed on three-dimensional hierarchically-structured indium tin oxide electrodes [28,29].…”

Section: Pioa Is Redox Active Between +250 and −400 MV Versus Shementioning

confidence: 99%

His/Met heme ligation in the PioA outer membrane cytochrome enabling light-driven extracellular electron transfer by Rhodopseudomonas palustris TIE-1

Edwards

Blake

et al. 2020

Nanotechnology

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A growing number of bacterial species are known to move electrons across their cell envelopes. Naturally this occurs in support of energy conservation and carbon-fixation. For biotechnology it allows electron exchange between bacteria and electrodes in microbial fuel cells and during microbial electrosynthesis. In this context Rhodopseudomonas palustris TIE-1 is of much interest. These bacteria respond to light by taking electrons from their external environment, including electrodes, to drive CO2-fixation. The PioA cytochrome, that spans the bacterial outer membrane, is essential for this electron transfer and yet little is known about its structure and electron transfer properties. Here we reveal the ten c-type hemes of PioA are redox active across the window +250 to −400 mV versus Standard Hydrogen Electrode and that the hemes with most positive reduction potentials have His/Met and His/H2O ligation. These chemical and redox properties distinguish PioA from the more widely studied family of MtrA outer membrane decaheme cytochromes with ten His/His ligated hemes. We predict a structure for PioA in which the hemes form a chain spanning the longest dimension of the protein, from Heme 1 to Heme 10. Hemes 2, 3 and 7 are identified as those most likely to have His/Met and/or His/H2O ligation. Sequence analysis suggests His/Met ligation of Heme 2 and/or 7 is a defining feature of decaheme PioA homologs from over 30 different bacterial genera. His/Met ligation of Heme 3 appears to be less common and primarily associated with PioA homologs from purple non-sulphur bacteria belonging to the alphaproteobacteria class.

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Microperoxidase-11 modified mesoporous SnO₂ film electrodes for the detection of antimalarial drug artemisinin

Abstract: A simple and efficient preparation method for Microperoxidase-11 modified mesoporous SnO2 films on ITO glass substrates for the development of a sensitive electrochemical drug sensor for the determination of artemisinin.

Cited by 9 publications

References 39 publications

Electrocatalysis by Heme Enzymes—Applications in Biosensing

Electrocatalysis by Heme Enzymes—Applications in Biosensing

Electrochemical Biosensors Employing Natural and Artificial Heme Peroxidases on Semiconductors

His/Met heme ligation in the PioA outer membrane cytochrome enabling light-driven extracellular electron transfer by Rhodopseudomonas palustris TIE-1

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Microperoxidase-11 modified mesoporous SnO2 film electrodes for the detection of antimalarial drug artemisinin

Abstract: A simple and efficient preparation method for Microperoxidase-11 modified mesoporous SnO2 films on ITO glass substrates for the development of a sensitive electrochemical drug sensor for the determination of artemisinin.

Cited by 9 publications

References 39 publications

Electrocatalysis by Heme Enzymes—Applications in Biosensing

Electrocatalysis by Heme Enzymes—Applications in Biosensing

Electrochemical Biosensors Employing Natural and Artificial Heme Peroxidases on Semiconductors

His/Met heme ligation in the PioA outer membrane cytochrome enabling light-driven extracellular electron transfer by Rhodopseudomonas palustris TIE-1

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Microperoxidase-11 modified mesoporous SnO₂ film electrodes for the detection of antimalarial drug artemisinin