Hydroquinone diphosphate/Ag + as an enzymatic substrate for alkaline phosphatase catalyzed silver deposition

Neves, Marta M.P.S.; García, María Begoña González; Santos, David Hernández; Fanjul‐Bolado, Pablo

doi:10.1016/j.elecom.2015.07.015

Cited by 8 publications

(3 citation statements)

References 16 publications

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“…It is known that Ag undergoes oxidative etching in the presence of oxygen (eqn (1)), 22 and that Ag + ions can be reduced by HQ to give Ag and 1,4-benzoquinone (BQ; eqn (2)). 23 Their reduction potentials were estimated based on the reaction conditions (pH = 5.8; [Ag + ] residual = 0.1 mM) to be 0.33 V and 0.21 V, respectively. The sum of the two equations gives eqn (3) by canceling the Ag species, suggesting that Ag effectively plays the role of ''catalyst'' for the reaction between O 2 and HQ (Fig.…”

Section: Resultsmentioning

confidence: 99%

A facile route to Janus nanorods via redox-assisted ripening

Sun¹,

Wang²,

Wu³

et al. 2023

Mater. Chem. Front.

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Section: Resultsmentioning

confidence: 99%

A facile route to Janus nanorods via redox-assisted ripening

Sun¹,

Wang²,

Wu³

et al. 2023

Mater. Chem. Front.

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“…In addition, the enzymatic product P can promote the formation of electroactive metal deposition on the electrode surface to produce a detectable electrochemical signal In this method, the enzymatic product P is regenerated from its oxidized form (Q) by th additional reducing substance RII. One of the most typical examples is enzymatic silve (Ag) biometallization, in which Ag + (OI) is reduced by the enzymatic product P into me tallic silver (RI) deposition on the solid substrate [65][66][67]. The electrochemical oxidation o the deposited Ag could produce a high electrochemical signal.…”

Section: Electrochemical-electrochemical Redox Cyclingmentioning

confidence: 99%

Overview on the Development of Electrochemical Immunosensors by the Signal Amplification of Enzyme- or Nanozyme-Based Catalysis Plus Redox Cycling

Xia,

Gao,

Zhang

et al. 2024

Molecules

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Enzyme-linked electrochemical immunosensors have attracted considerable attention for the sensitive and selective detection of various targets in clinical diagnosis, food quality control, and environmental analysis. In order to improve the performances of conventional immunoassays, significant efforts have been made to couple enzyme-linked or nanozyme-based catalysis and redox cycling for signal amplification. The current review summarizes the recent advances in the development of enzyme- or nanozyme-based electrochemical immunosensors with redox cycling for signal amplification. The special features of redox cycling reactions and their synergistic functions in signal amplification are discussed. Additionally, the current challenges and future directions of enzyme- or nanozyme-based electrochemical immunosensors with redox cycling are addressed.

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“…The present work describes two new electrochemical methods for the determination of ALP activity, one intended as a new analytical tool for biochemical research and a second intended more for use at point-of-care settings. The advancements presented here include (i) the stabilization of the otherwise unsteady anodic current of hydroquinone (HQ) at high pH for signal transduction from the ALP reaction, (ii) the first homogeneous kinetic data for ALP-triggered release of HQ from a substrate hydroquinone diphosphate (HQDP), − and (iii) the incubation-free and incubation-dependent electrochemical modes of ALP determination at a conventional glassy carbon electrode (GC) and commercial glucose test strip (GTS). The latter was chosen because it is a technology perfected for decades to provide a reliable electrical signal from small real-life samples (blood).…”

Section: Introductionmentioning

confidence: 99%

Electroanalysis of Enzyme Activity in Small Biological Samples: Alkaline Phosphatase

2021

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The discovery of sulfite-stabilized anodic current of hydroquinone (HQ) at high pH was used to develop two new methods for measuring the activity of the key biomarker alkaline phosphatase (ALP). Both approaches relied on the monitoring of ALP-triggered release of HQ from a substrate hydroquinone diphosphate (HQDP) into a pH 10.00 solution. One detected the released HQ via the internally calibrated electrochemical continuous enzyme assay (ICECEA) at a glassy carbon (GC) electrode with no sample incubation. The other used sample incubation with HQDP and quantified the released HQ via a coulometric assay at a commercial glucose test strip (GTS). The assay solution was optimized by investigating the ALP/HQDP/HQ system at a GC electrode. The ICECEA revealed high affinity of ALP for HQDP (K m app , 87 μM; V max , 0.36 μM min −1 ) and detected ALP down to 0.022 U L −1 . At GTS, ALP was detected down to 0.064 U L −1 in a 1 μL sample of human serum after a 20 min incubation at room temperature. The linear range (R 2 , 0.994) extended at least up to 1.7 U L −1 ALP, which covered more than the clinical range for ALP in serum. The interferences from the sample matrix including those from indigenous glucose were eliminated using a charge difference ΔQ (=Q total − Q sample matrix ) as a signal for ALP. Both advances proposed here are direct (no auxiliary enzymes or labels required), accurate (98 ± 3% ALP signal recovery), and precise (relative standard deviation (RSD), <7%). The HQDP-GTS-based assay advances the analysis of ALP activity in microsized real-life samples.

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Hydroquinone diphosphate/Ag + as an enzymatic substrate for alkaline phosphatase catalyzed silver deposition

Cited by 8 publications

References 16 publications

A facile route to Janus nanorods via redox-assisted ripening

A facile route to Janus nanorods via redox-assisted ripening

Overview on the Development of Electrochemical Immunosensors by the Signal Amplification of Enzyme- or Nanozyme-Based Catalysis Plus Redox Cycling

Electroanalysis of Enzyme Activity in Small Biological Samples: Alkaline Phosphatase

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