Cofactor-specific covalent anchoring of cytochrome b<sub>562</sub>on a single-walled carbon nanotube by click chemistry

Onoda, Akira; Inoue, Nozomu; Campidelli, Stéphane; Hayashi, Takashi

doi:10.1039/c6ra14195a

Cited by 9 publications

(8 citation statements)

References 48 publications

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“…Redox active biomolecules (cytochrome b 562 ) covalently attached on carbon nanotubes have also been visualized by AFM. [51] To the best of our knowledge, this has not been realized so far for enzymes. This latter technique can provide much more information about enzyme coverage, thickness of the enzyme layer and even visualization of single enzyme molecules.…”

Section: Afmmentioning

confidence: 97%

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Micro‐ and Nanoscopic Imaging of Enzymatic Electrodes: A Review

2019

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Redox enzymes, which catalyze electron transfer reactions in living organisms, can be used as selective and sensitive bioreceptors in biosensors, or as efficient catalysts in biofuel cells. In these bioelectrochemical devices, the enzymes are immobilized at a conductive surface, the electrode, with which they must be able to exchange electrons. Different physicochemical methods have been coupled to electrochemistry to characterize the enzyme‐modified electrochemical interface. In this Review, we summarize most efforts performed to investigate the enzymatic electrodes at the micro‐ and even nanoscale, thanks to microscopy techniques. Contrary to electrochemistry, which gives only a global information about all processes occurring at the electrode surface, microscopy offers a spatial resolution. Several techniques have been implemented; mostly scanning probe microscopies like atomic force microscopy, scanning tunneling microscopy, and scanning electrochemical microscopy, but also scanning electron microscopy and fluorescence microscopy. These studies demonstrate that various information can be obtained thanks to microscopy at different scales. Electrode imaging has been performed to confirm the presence of enzymes, to quantify and localize the biomolecules, but also to evaluate the morphology of immobilized enzymes, their possible conformation changes upon turnover, and their orientation at the electrode surface. Local redox activity has also been imaged and kinetics has been resolved.

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Section: Afmmentioning

confidence: 97%

“…Redox active biomolecules (cytochrome b 562 ) covalently attached on carbon nanotubes have also been visualized by AFM . To the best of our knowledge, this has not been realized so far for enzymes.…”

Section: Electrode Imaging To Confirm the Presence Of Enzymesmentioning

confidence: 99%

Micro‐ and Nanoscopic Imaging of Enzymatic Electrodes: A Review

2019

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“…In some instances, redox‐active cofactors can be synthesized and incorporated into so‐called cofactor‐free “apo‐proteins.” This offers a route to generating redox proteins containing modified redox cofactors that have chemical functionalities complementary to those which can be added to the electrode surface. For example, incorporation of an azide‐functionalized heme group into cytochrome b562 enabled copper(I)‐catalyzed azide–alkyne cycloaddition to an alkyne‐functionalized CNT immobilized onto a GC electrode . Alternatively, for proteins containing metal‐electron entry/exit sites that have multiple ligands, genetic removal of an amino acid ligand residue offers the opportunity for structural reconstitution of the redox protein with an external ligand that is tethered to the electrode surface.…”

Section: Crosslinking Strategies For Site‐specifically Connecting Promentioning

confidence: 99%

“…For example, incorporation of an azide-functionalized heme group into cytochrome b562 enabled copper(I)-catalyzed azide-alkyne cycloaddition to an alkyne-functionalized CNT immobilized onto aG Ce lectrode. [184] Alternatively,f or proteins containing metal-electron entry/exit sites that have multiple ligands,g enetic removal of an amino acid ligand residue offers the opportunity for structuralr econstitution of the redoxp rotein with an external ligand that is tethered to the electrode surface. This strategy has been demonstrated for an azurin variant.…”

Section: Cofactor Ligationmentioning

confidence: 99%

Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces

Yates

Fascione

Parkin

2018

Chemistry A European J

104

116

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The immobilization of redox proteins or enzymes onto conductive surfaces has application in the analysis of biological processes, the fabrication of biosensors, and in the development of green technologies and biochemical synthetic approaches. This review evaluates the methods through which redox proteins can be attached to electrode surfaces in a “wired” configuration, that is, one that facilitates direct electron transfer. The feasibility of simple electroactive adsorption onto a range of electrode surfaces is illustrated, with a highlight on the recent advances that have been achieved in biotechnological device construction using carbon materials and metal oxides. The covalent crosslinking strategies commonly used for the modification and biofunctionalization of electrode surfaces are also evaluated. Recent innovations in harnessing chemical biology methods for electrically wiring redox biology to surfaces are emphasized.

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“…Campidelli [46] revised the application of CuAAC for CNT functionalization. In a more recent example, redox-active cytochrome b562 and a tethered azide group on the heme propionate side chain (cyt1) were covalently linked to an acetylene moiety introduced on the sidewall of single-wall carbon nanotubes (SWCNTs) by copper-catalyzed click chemistry (Figure 3A), forming a triazole ring with the heme active site directly linked to the carbon nanotubes [47]. CuAAC was also used in multi-walled carbon nanotubes (MWCNTs) functionalization with β-cyclodextrins (β-CDs) [48].…”

Section: Preparation Of Electrochemical Platformsmentioning

confidence: 99%

Copper(I)-Catalyzed Click Chemistry as a Tool for the Functionalization of Nanomaterials and the Preparation of Electrochemical (Bio)Sensors

Yáñez‐Sedeño

González‐Cortés

Campuzano

et al. 2019

Sensors

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Proper functionalization of electrode surfaces and/or nanomaterials plays a crucial role in the preparation of electrochemical (bio)sensors and their resulting performance. In this context, copper(I)-catalyzed azide-alkyne cycloaddition (CuAAC) has been demonstrated to be a powerful strategy due to the high yields achieved, absence of by-products and moderate conditions required both in aqueous medium and under physiological conditions. This particular chemistry offers great potential to functionalize a wide variety of electrode surfaces, nanomaterials, metallophthalocyanines (MPcs) and polymers, thus providing electrochemical platforms with improved electrocatalytic ability and allowing the stable, reproducible and functional integration of a wide range of nanomaterials and/or different biomolecules (enzymes, antibodies, nucleic acids and peptides). Considering the rapid progress in the field, and the potential of this technology, this review paper outlines the unique features imparted by this particular reaction in the development of electrochemical sensors through the discussion of representative examples of the methods mainly reported over the last five years. Special attention has been paid to electrochemical (bio)sensors prepared using nanomaterials and applied to the determination of relevant analytes at different molecular levels. Current challenges and future directions in this field are also briefly pointed out.

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Cofactor-specific covalent anchoring of cytochrome b₅₆₂on a single-walled carbon nanotube by click chemistry

Abstract: Redox-active cytochromeb562with a tethered azide group on the heme propionate side chain is covalently linked to an acetylene moiety introduced on the sidewall of a single-walled carbon nanotube by copper-catalyzed click chemistry.

Cited by 9 publications

References 48 publications

Micro‐ and Nanoscopic Imaging of Enzymatic Electrodes: A Review

Micro‐ and Nanoscopic Imaging of Enzymatic Electrodes: A Review

Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces

Copper(I)-Catalyzed Click Chemistry as a Tool for the Functionalization of Nanomaterials and the Preparation of Electrochemical (Bio)Sensors

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Cofactor-specific covalent anchoring of cytochrome b562on a single-walled carbon nanotube by click chemistry

Abstract: Redox-active cytochromeb562with a tethered azide group on the heme propionate side chain is covalently linked to an acetylene moiety introduced on the sidewall of a single-walled carbon nanotube by copper-catalyzed click chemistry.

Cited by 9 publications

References 48 publications

Micro‐ and Nanoscopic Imaging of Enzymatic Electrodes: A Review

Micro‐ and Nanoscopic Imaging of Enzymatic Electrodes: A Review

Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces

Copper(I)-Catalyzed Click Chemistry as a Tool for the Functionalization of Nanomaterials and the Preparation of Electrochemical (Bio)Sensors

Contact Info

Product

Resources

About

Cofactor-specific covalent anchoring of cytochrome b₅₆₂on a single-walled carbon nanotube by click chemistry