What can electrochemistry tell us about individual enzymes?

Davis, Connor; Wang, Stephanie X.; Sepunaru, Lior

doi:10.1016/j.coelec.2020.100643

Cited by 11 publications

(9 citation statements)

References 78 publications

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“…Also, the dynamics and catalytic activity of single enzymes could be tracked by an enzymatically enhanced current. 24 The third type relies on the electrolysis collisions of individual entities. The collision between entities and an electrode initiates the electrooxidation/electro-reduction of the former.…”

Section: Electrochemistrymentioning

confidence: 99%

Mass Transport and Electron Transfer at the Electrochemical-Confined Interface

Chen

Wang

et al. 2023

J. Phys. Chem. Lett.

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Single entity measurements based on the stochastic collision electrochemistry provide a promising and versatile means to study single molecules, single particles, single droplets, etc. Conceptually, mass transport and electron transfer are the two main processes at the electrochemically confined interface that underpin the most transient electrochemical responses resulting from the stochastic and discrete behaviors of single entities at the microscopic scale. This perspective demonstrates how to achieve controllable stochastic collision electrochemistry by effectively altering the two processes. Future challenges and opportunities for stochastic collision electrochemistry are also highlighted.

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Section: Electrochemistrymentioning

confidence: 99%

Mass Transport and Electron Transfer at the Electrochemical-Confined Interface

Chen

Wang

et al. 2023

J. Phys. Chem. Lett.

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“…Electrochemistry, and especially bioelectrochemistry, has great potential in the field of enzymology and determination of such events as substrate binding, the oxidation state of the catalytic center, and structural fluctuations [12,13].…”

Section: Introductionmentioning

confidence: 99%

Electroenzymatic Model System for the Determination of Catalytic Activity of Erwinia carotovora L-Asparaginase

et al. 2022

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An electrochemical method for the determination of the catalytic activity of L-asparaginase (ASNase) from Erwinia carotovora was proposed. Our approach is based on the electrooxidation of amino acids from L-asparaginase polypeptide backbones. The electrochemical behavior of ASNase on electrodes obtained by screen-printing modified with single-wall carbon nanotubes (SPE/SWCNTs) as sensing elements demonstrated a broad oxidation peak at 0.5–0.6 V centered at 0.531 ± 0.010 V. We have shown that in the presence of the substrate L-asparagine, the oxidation current of the enzyme was reduced in a concentration-dependent manner. The specificity of electrochemical analysis was confirmed in experiments with glycine, an amino acid with no substrate activity on ASNase and does not reduce the oxidation peak of L-asparaginase. The addition of glycine did not significantly influence the amplitude of the oxidation current. The innovative aspects of the proposed electrochemical sensor are the direct monitoring of ASNase catalytic activity and a reagentless approach, which does not require additional reagents or labels.

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“…The functionality of metalloproteins is universally attributed to the presence metal-based active sites. , Over the past few decades, electrochemistry has emerged as one of the most efficient tools for understanding structure–function relationships in metalloproteins. − Recently, we investigated the effects of local coordination of amino acids on heme electrochemistry to evaluate that interaction geometry and spin state differences between reduced and oxidized forms play an important role in controlling redox reversibility . However, from electrochemistry alone, we cannot elucidate how the local structure around the iron center evolves with change in redox state.…”

Section: Introductionmentioning

confidence: 99%

Structure-Redox Response Correlation in a Few Select Heme Systems Using X-ray Absorption Spectroelectrochemistry

Samajdar

Bhattacharyya

2021

J. Phys. Chem. B

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Heme based biomolecules control some of the most crucial life processes, such as oxygen and electron transport during respiration and energy metabolism, respectively. The active site of the heme, viz., the metal center, plays a key role and attributes functionality to these biomolecules. During the oxygen binding and debinding processes, it is important to note that the oxidation state of iron in hemoglobin (+II in the native form) does not undergo any change. However, the spin states of the metal center change. We present here a comprehensive study of the redox response of such molecules, based on the electronic structure of the active site. The local electronic structure of heme in a few selective molecular systems is studied in operando via synchrotron Xray absorption spectroscopy (Fe K-edge) and cyclic voltammetry. Our objective is to identify the electronic structural parameters that can effectively be correlated with the redox reversibility. Evolution in these parameters can be followed to trace the overall changes in redox state of the system. Our data indicate that axial coordination and spin state of the iron center are two such parameters that are intimately connected with the redox response.

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What can electrochemistry tell us about individual enzymes?

Cited by 11 publications

References 78 publications

Mass Transport and Electron Transfer at the Electrochemical-Confined Interface

Mass Transport and Electron Transfer at the Electrochemical-Confined Interface

Electroenzymatic Model System for the Determination of Catalytic Activity of Erwinia carotovora L-Asparaginase

Structure-Redox Response Correlation in a Few Select Heme Systems Using X-ray Absorption Spectroelectrochemistry

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