A π–π Bonding-Assisted Molecular-Wiring of Folded-Cytochrome c and Naphthoquinone and Its Electron-Relay-Based Bioelectrocatalytic H2O2 Reduction Reaction Visualized by Redox-Competitive Scanning Electrochemical Microscopy
The electron-transfer (ET) reaction of cytochrome c (Cytc) protein with biomolecules is a cutting-edge research area of interest in understanding the functionalities of natural systems. Several electrochemical biomimicking studies based on Cytc-protein-modified electrodes prepared via electrostatic...
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Published in | Langmuir Vol. 39; no. 33; pp. 11556 - 11570 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
American Chemical Society
22.08.2023
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Online Access | Get full text |
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Summary: | The electron-transfer (ET) reaction of cytochrome c (Cytc) protein with biomolecules is a cutting-edge research area of interest in understanding the functionalities of natural systems. Several electrochemical biomimicking studies based on Cytc-protein-modified electrodes prepared via electrostatic interaction and covalent bonding approaches have been reported. Indeed, natural enzymes involve multiple types of bonding, such as hydrogen, ionic, covalent, and π–π, etc. In this work, we explore a Cytc-protein chemically modified glassy carbon electrode (GCE/CB@NQ/Cytc) prepared via π–π bonding using graphitic carbon as an underlying surface and an aromatic organic molecule, naphthoquinone (NQ), as a cofactor for an effective ET reaction. A simple drop-casting technique-based preparation of GCE/CB@NQ showed a distinct surface-confined redox peak at a standard electrode potential (E°) = −0.2 V vs Ag/AgCl (surface excess = 21.3 nmol cm–2) in pH 7 phosphate buffer solution. A control experiment of modification of NQ on an unmodified GCE failed to show any such unique feature. For the preparation of GCE/CB@NQ/Cytc, a dilute solution of Cytc–pH 7 phosphate buffer was drop-cast on the GCE/CB@NQ surface, wherein the protein folding and denaturalization-based complication and its associated ET functionalities were avoided. Molecular dynamics simulation studies show the complexation of NQ with Cytc at the protein binding sites. The protein-bound surface shows an efficient and selective bioelectrocatalytic reduction performance of H2O2, as demonstrated using cyclic voltammetry and amperometric i–t techniques. Finally, the redox-competition scanning electrochemical microscopy (RC-SECM) technique was adopted for in situ visualization of the electroactive adsorbed surface. The RC-SECM images clearly show the regions of highly bioelectrocatalytic active sites of Cytc-proteins bound to NQ molecules on a graphitic carbon surface. The binding of Cytc with NQ has significant implications for studying the biological electron transport mechanism, and the proposed method provides the requisite framework for such a study. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0743-7463 1520-5827 |
DOI: | 10.1021/acs.langmuir.3c00941 |