Electron transfer, conduction and biorecognition properties of the redox metalloprotein Azurin assembled onto inorganic substrates

Baldacchini, Chiara; Bizzarri, Anna Rita; Cannistraro, Salvatore

doi:10.1016/j.eurpolymj.2016.04.030

Cited by 34 publications

(36 citation statements)

References 146 publications

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“…[10] TheA u-bound CytC mutant (E104C) yields oriented monolayers, sufficientlyrobust to carry out solid-state electron-transport measurements [19] at both room and cryogenic temperatures( approximately 10-15 K). Briefly, mm-sized Au electrodepairs were fabricated on aSiwafer by photolithography.M onolayers of CytC(E104C) were prepared by using the surface-exposed cysteine 104 residue that binds covalently to the micro-fabricated Au electrodei ns uch aw ay that its hemin is proximal to the top Au nanowire (AuNW) electrode( 0.8-0.9nm between the Fe III ion and the physical top contact).…”

Section: Methodsmentioning

confidence: 99%

“…Briefly, mm-sized Au electrodepairs were fabricated on aSiwafer by photolithography.M onolayers of CytC(E104C) were prepared by using the surface-exposed cysteine 104 residue that binds covalently to the micro-fabricated Au electrodei ns uch aw ay that its hemin is proximal to the top Au nanowire (AuNW) electrode( 0.8-0.9nm between the Fe III ion and the physical top contact). [10] TheA u-bound CytC mutant (E104C) yields oriented monolayers, sufficientlyrobust to carry out solid-state electron-transport measurements [19] at both room and cryogenic temperatures( approximately 10-15 K). [20] The protein monolayers were characterized by ellipsometry and atomic force microscopy (thickness), UV/Vis,a nd PM-IRRAS spectroscopies (Supporting Information,F igure S3).…”

Section: Methodsmentioning

confidence: 99%

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A Solid‐State Protein Junction Serves as a Bias‐Induced Current Switch

et al. 2019

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As ample-type protein monolayer,t hat can be as tepping stone to practical devices,c an behave as an electrically driven switch. This feat is achieved using ar edox protein, cytochrome C( CytC), with its heme shielded from direct contact with the solid-state electrodes.A binitio DFT calculations,c arried out on the CytC-Aus tructure,s howt hat the coupling of the heme,t he origin of the protein frontier orbitals,tothe electrodes is sufficiently weak to prevent Fermi level pinning.T hus,e xternal bias can bring these orbitals in and out of resonance with the electrode.Using acytochrome C mutant for direct SÀAu bonding,a pproximately 80 %o ft he Au-CytC-Au junctions showatgreater than 0.5 Vbias aclear conductance peak, consistent with resonant tunneling.The onoff change persists up to room temperature,d emonstrating reversible,b ias-controlled switching of ap rotein ensemble, which,with its built-in redundancy,provides arealistic path to protein-based bioelectronics.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

A Solid‐State Protein Junction Serves as a Bias‐Induced Current Switch

et al. 2019

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“…Over the past decades, redox proteins with transition metal ion centers with variable valence were integrated into solid-state electronic junctions for electron transport (ETp) measurements (3)(4)(5)(6). Apart from the fundamental interest in understanding solid-state ETp properties of proteins, their integration into hybrid junctions might lead to devices with designed electronic functions, a holy grail of bioelectronics (7,8). Previous studies of the blue copper protein azurin (Az) containing junctions, with single, several (9-11), or multiple protein molecules (12), have suggested that the efficiency of their ETp is comparable with that via conjugated organic molecules as judged from the observed current densities at low bias (100 mV) (4).…”

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confidence: 99%

Tunneling explains efficient electron transport via protein junctions

Fereiro

Pecht

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

136

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Metalloproteins, proteins containing a transition metal ion cofactor, are electron transfer agents that perform key functions in cells. Inspired by this fact, electron transport across these proteins has been widely studied in solid-state settings, triggering the interest in examining potential use of proteins as building blocks in bioelectronic devices. Here, we report results of low-temperature (10 K) electron transport measurements via monolayer junctions based on the blue copper protein azurin (Az), which strongly suggest quantum tunneling of electrons as the dominant charge transport mechanism. Specifically, we show that, weakening the protein-electrode coupling by introducing a spacer, one can switch the electron transport from off-resonant to resonant tunneling. This is a consequence of reducing the electrode's perturbation of the Cu(II)-localized electronic state, a pattern that has not been observed before in protein-based junctions. Moreover, we identify vibronic features of the Cu(II) coordination sphere in transport characteristics that show directly the active role of the metal ion in resonance tunneling. Our results illustrate how quantum mechanical effects may dominate electron transport via protein-based junctions.

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“…The study of electron transport through biomolecules in solidstate junctions aims at shedding new light on charge transfer in these systems, which is a fundamental process underlying many biological functions such as respiration, photosynthesis, enzymatic processes, and cellular signal transduction. 1 This field of "biomolecular electronics" presently receives much attention, [2][3][4][5][6][7][8][9][10][11][12][13][14][15] and the hope is to build novel bio-inspired electronic devices that exploit the versatile chemical properties of biomolecules. For instance, electron transport via peptide matrices in proteins has been found to be surprisingly fast and efficient, 16 which may allow us to create electronic devices incorporating proteins, where conductance properties can be tailored by chemical modification.…”

Section: Introductionmentioning

confidence: 99%

Doping hepta-alanine with tryptophan: A theoretical study of its effect on the electrical conductance of peptide-based single-molecule junctions

Schosser

Zotti

Cuevas

et al. 2019

The Journal of Chemical Physics

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Motivated by a recent experiment [C. Guo et al., Proc. Natl. Acad. Sci. U. S. A. 113, 10785 (2016)], we carry out a theoretical study of electron transport through peptide-based single-molecule junctions. We analyze the pristine hepta-alanine and its functionalizations with a single tryptophan unit, which is placed in three different locations along the backbone. Contrary to expectations from the experiment on self-assembled monolayers, we find that insertion of tryptophan does not raise the electrical conductance and that the resulting peptides instead remain insulating in the framework of a coherent transport picture. The poor performance of these molecules as conductors can be ascribed to the strongly off-resonant transport and low electrode-molecule coupling of the frontier orbitals. Although the introduction of tryptophan increases the energy of the highest occupied molecular orbital (HOMO) of the peptides in the gas phase, the new HOMO states are localized on the tryptophan unit and therefore essentially do not contribute to coherent charge transport.Published under license by AIP Publishing. https://doi.

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Electron transfer, conduction and biorecognition properties of the redox metalloprotein Azurin assembled onto inorganic substrates

Cited by 34 publications

References 146 publications

A Solid‐State Protein Junction Serves as a Bias‐Induced Current Switch

A Solid‐State Protein Junction Serves as a Bias‐Induced Current Switch

Tunneling explains efficient electron transport via protein junctions

Doping hepta-alanine with tryptophan: A theoretical study of its effect on the electrical conductance of peptide-based single-molecule junctions

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