Supramolecular electrode assemblies for bioelectrochemistry

Laftsoglou, Theodoros; Jeuken, Lars J. C.

doi:10.1039/c7cc01154g

Cited by 15 publications

(19 citation statements)

References 74 publications

(87 reference statements)

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“…Multiheme cytochromes display interesting catalytic properties, such as nitrite reduction or ammonia oxidation, involving intramolecular electron transfer steps that were extensively investigated. [29,71,[98][99][100] In particular, Raman resonance (RR) spectroscopy, surface enhanced resonance Raman spectroscopy (SERRS) and surfaceenhanced infrared spectroscopy (SEIRA) are very reliable techniques to this end. [87][88][89] In most cases, however, the protein is not used in the purified form, but the devices employ biofilms in which these proteins play a crucial role in extracellular electron transfer.…”

Section: Heme Proteinsmentioning

confidence: 99%

“…[30] For this reason, synthetic proteins obtained starting from myoglobin through side directed mutagenesis have been produced, which showed good electrocatalytic properties. [28,29,100] Two procedures result particularly efficient: the layer-by-layer assembly [36,[108][109][110][111][112][113][114][115][116] and the immobilization in lipid bilayer membranes. However, immobilization can induce more or less extended unfolding.…”

Section: Heme Proteinsmentioning

confidence: 99%

“…[92,93] Several immobilized heme proteins yield well-defined electrochemical and electrocatalytic responses. [100,[117][118][119] The most extensively used heme proteins for bioelectrocatalysis are mutated and unfolded cytochromes c, myoglobins, hemoglo-bins, peroxidases, catalases, cytochrome P450, microperoxidases (Table 1). In particular, heme b is partially or completely released from the protein in case the immobilization conditions are not appropriate: as a result, the protein loses its properties and the electrochemical response is due to a non-native form of the protein or to the heme group in solution.…”

Section: Heme Proteinsmentioning

confidence: 99%

“…It consists of a single polypeptide chain wrapped to form 8 alphahelixes. [29,30,71,76,94,100] Several procedures have been developed to retain the folding for the electrode-immobilized. In physiological conditions myoglobin contains a single ferrous heme b.…”

Section: Myoglobin and Hemoglobinmentioning

confidence: 99%

“…[28,29,[95][96][97] In these cases, spectroscopic measurements demonstrate the integrity of the protein immobilized on the electrode. [29,71,[98][99][100] In particular, Raman resonance (RR) spectroscopy, surface enhanced resonance Raman spectroscopy (SERRS) and surfaceenhanced infrared spectroscopy (SEIRA) are very reliable techniques to this end. [30,101,102] Such an approach is highly specific and sensitive and allows unambiguous assessment of the redox, coordination, and spin state of the heme group.…”

Section: Heme Proteinsmentioning

confidence: 99%

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Electrocatalytic Properties of Immobilized Heme Proteins: Basic Principles and Applications

et al. 2019

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Heme proteins encompass redox enzymes, electron transferases, and species for dioxygen transport and storage. Upon immobilization on a conductive surface, heme proteins can accomplish bioelectrocatalysis. In this process, they carry out oxidation or reduction of substrates at a solid electrode acting as electron acceptor or donor, respectively, thanks to electron transfer processes occurring at the interphase. The efficiency of bioelectrocatalysis depends on the electrical communication of the protein with the electrode surface, retention of protein structure upon adsorption and accessibility of the substrate to the active site. This Minireview outlines the main factors affecting bioelectrocatalysis by adsorbed heme proteins, highlights open issues, and summarizes recent advances in the field.

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Section: Heme Proteinsmentioning

confidence: 99%

Section: Heme Proteinsmentioning

confidence: 99%

Section: Heme Proteinsmentioning

confidence: 99%

Section: Myoglobin and Hemoglobinmentioning

confidence: 99%

Section: Heme Proteinsmentioning

confidence: 99%

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Electrocatalytic Properties of Immobilized Heme Proteins: Basic Principles and Applications

et al. 2019

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In Situ and Operando Techniques for Investigating Electron Transfer in Biological Systems

et al. 2020

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When bioelectrochemistry meets other analytical techniques for in situ experiments, new possibilities for understanding the nature of charge‐transfer reactions are provided. Despite progress in recent years in analytical instrumentation, a number of key issues remains for bioelectrochemistry, in terms of the mechanistic description of the surface reactions involved in biomolecules’ electron transfer. The main challenges of these techniques are the concomitant detection of electron transfer and molecular alteration as well as the development of suitable bioelectrodes. This review discusses the most recent and emerging in situ and operando electrochemical methods used to study biological systems such as redox proteins, nucleic acids, small biomolecules, cells, and biomembranes, focusing on electrochemical methods coupled with spectroscopic, spectrometric, and microscopic techniques.

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Mimicking Photosystem I with a Transmembrane Light Harvester and Energy Transfer‐Induced Photoreduction in Phospholipid Bilayers

Pannwitz

Saaring

Beztsinna

et al. 2020

Chemistry A European J

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Photosystem I (PS I) is a transmembrane protein that assembles perpendicular to the membrane, and performs light harvesting, energy transfer, and electron transfer to a final, water‐soluble electron acceptor. We present here a supramolecular model of it formed by a bicationic oligofluorene 12+ bound to the bisanionic photoredox catalyst eosin Y (EY2−) in phospholipid bilayers. According to confocal microscopy, molecular modeling, and time dependent density functional theory calculations, 12+ prefers to align perpendicularly to the lipid bilayer. In presence of EY2−, a strong complex is formed (Ka=2.1±0.1×106 m−1), which upon excitation of 12+ leads to efficient energy transfer to EY2−. Follow‐up electron transfer from the excited state of EY2− to the water‐soluble electron donor EDTA was shown via UV–Vis absorption spectroscopy. Overall, controlled self‐assembly and photochemistry within the membrane provides an unprecedented yet simple synthetic functional mimic of PS I.

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Supramolecular electrode assemblies for bioelectrochemistry

Abstract: Supramolecular approaches in bioelectrochemistry have boosted enzyme loading on electrodes and shaped biocompatible environments for enzymes.

Cited by 15 publications

References 74 publications

Electrocatalytic Properties of Immobilized Heme Proteins: Basic Principles and Applications

Electrocatalytic Properties of Immobilized Heme Proteins: Basic Principles and Applications

In Situ and Operando Techniques for Investigating Electron Transfer in Biological Systems

Mimicking Photosystem I with a Transmembrane Light Harvester and Energy Transfer‐Induced Photoreduction in Phospholipid Bilayers

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