Molecularly-Resolved Bioelectronics

Davis, Jason J.; Peters, Ben; Xi, Wang; Axford, Daniel

doi:10.2174/157341308783591825

Cited by 3 publications

(3 citation statements)

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“…[22][23][24][25][26][27] Though they inherently contain information on dispersion present within any given molecular population and enable a direct "visualization" of redox potentials, these experiments and their subsequent theoretical analyses remain demanding. 21,28,29 Molecular scale information can be acquired in the far field by fluorescence microscopy with relative ease under a variety of controllable solution-phase conditions. The emission intensity and lifetime from surface-confined molecules can, for example, be measured and related to conformation dynamics.…”

Section: Introductionmentioning

confidence: 99%

“…To move redox analyses to a more molecularly refined scale, a number of approaches involving nanoelectrodes and proximal probe configurations have been tabled. − By combining the near-field imaging resolution of scanning tunneling (STM) or conductive probe atomic force (CPAFM) microscopy with electrochemical potential control, for example, it has been possible to obtain high-resolution conductance images of electrode-confined protein molecules and to carry out functional mapping based on current/voltage and conductance/surface potential relationships. Observations possible within such experimental formats generate a wealth of information about surface homogeneity, molecular conductance, redox site coupling to electrodes, and switching potentials at truly molecular scales. − Though they inherently contain information on dispersion present within any given molecular population and enable a direct “visualization” of redox potentials, these experiments and their subsequent theoretical analyses remain demanding. ,, Molecular scale information can be acquired in the far field by fluorescence microscopy with relative ease under a variety of controllable solution-phase conditions. The emission intensity and lifetime from surface-confined molecules can, for example, be measured and related to conformation dynamics. , At appropriate levels of surface dilution (on optically transparent matrixes) molecular scale information initially hidden in ensemble-based analyses is resolved. − …”

Section: Introductionmentioning

confidence: 99%

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Visualizing and Tuning Thermodynamic Dispersion in Metalloprotein Monolayers

Patil

Davis

2010

J. Am. Chem. Soc.

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In coupling the redox state of an adsorbed molecule to its spectral characteristics redox profiles can be directly imaged by means of far-field fluorescence. At suitable levels of dilution, on optically transparent electrode surfaces, reversible interfacial electron transfer processes can be followed pixel by pixel down to scales which approach the molecular. In mapping out switching potentials across a surface population, thermodynamic dispersion, related to variance in the orientation, electronic coupling, protein fold, electric field drop, and general surface order, can be quantified. The self-assembled monolayer buffering the protein from the underlying metallic electrode surface not only acts to tune electronic coupling between the two but also potentially provides a variable more easily segmented from other contributions to molecular dispersion. We have, specifically, considered the possibility that the supporting monolayer crystallinity is a significant contributor to the subsequently observed spread in half-wave potentials. We report here that this is indeed the case and that this spread diminishes from 17 to 12 mV for the blue copper protein azurin as the supporting alkanethiol layer crystallinity increases. The work herein, then, presents not only a direct determination of submonolayer scale variance in redox character but also a means of tuning this through gross surface and entirely standard chemical means.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Visualizing and Tuning Thermodynamic Dispersion in Metalloprotein Monolayers

Patil

Davis

2010

J. Am. Chem. Soc.

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“…In this respect, macromolecules − and solid-state biomolecules in particular − offer useful advantages. Upon hosting foreign species, fine changes in the macromolecule properties can potentially be achieved with minimal effect on their structural and assembly characteristics.…”

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confidence: 99%

Doped Biomolecules in Miniaturized Electric Junctions

Mentovich¹,

Belgorodsky²,

Gozin³

et al. 2012

J. Am. Chem. Soc.

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Control over molecular scale electrical properties within nano junctions is demonstrated, utilizing site-directed C(60) targeting into protein macromolecules as a doping means. The protein molecules, self-assembled in a miniaturized transistor device, yield robust and reproducible operation. Their device signal is dominated by an active center that inverts affinity upon guest incorporation and thus controls the properties of the entire macromolecule. We show how the leading routes of electron transport can be drawn, spatially and energetically, on the molecular level and, in particular, how the dopant effect is dictated by its "strategic" binding site. Our findings propose the extension of microelectronic methodologies to the nanometer scale and further present a promising platform for ex situ studies of biochemical processes.

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