An electrochemical biosensor for the detection of tyrosine oxidation induced by Fenton reaction

Qu, Na; Guo, Liang-Hong; Zhu, Ben-Zhan

doi:10.1016/j.bios.2010.09.054

Cited by 43 publications

(23 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the case of TFBQ/H 2 O 2 , the photocurrent decreased to 27% of the blank, mostly likely due to severe DNA damage by the highly reactive HO • radicals. In our previous work [33], the surface concentration of PDDA before and after it was exposed to the Fenton reagents was assessed by XPS, and no change was found. It suggests PDDA was not damaged by HO • radicals.…”

Section: Resultsmentioning

confidence: 99%

Development of microplate-based photoelectrochemical DNA biosensor array for high throughput detection of DNA damage

Liu

Jia

Guo

2012

Sensors and Actuators B: Chemical

Self Cite

View full text Add to dashboard Cite

Section: Resultsmentioning

confidence: 99%

Development of microplate-based photoelectrochemical DNA biosensor array for high throughput detection of DNA damage

Liu

Jia

Guo

2012

Sensors and Actuators B: Chemical

Self Cite

View full text Add to dashboard Cite

“…In our previous study, an electrochemical biosensor was developed to detect tyrosine and protein oxidation induced by Fenton reagents. 20 The electrochemical signal of peptide on biosensor decreased remarkably after reaction with Fenton reagents, which are known to produce the highly reactive HO…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…20 We found that tyrosine in peptide was oxidized and the electrochemical signal of the peptide decreased markedly after incubation with Fenton reagents. When we extended our studies from the classic iron-mediated Fenton system to the new TXBQ-mediated organic Fenton-like system, we expected that the results should be similar.…”

Section: ■ Introductionmentioning

confidence: 94%

The Unexpected and Exceptionally Facile Chemical Modification of the Phenolic Hydroxyl Group of Tyrosine by Polyhalogenated Quinones under Physiological Conditions

Shao

et al. 2016

Chem. Res. Toxicol.

Self Cite

View full text Add to dashboard Cite

ABSTRACT:The phenolic hydroxyl group of tyrosine residue plays a crucial role in the structure and function of many proteins. However, little study has been reported about its modification by chemical agents under physiological conditions. In this study, we found, unexpectedly, that the phenolic hydroxyl group of tyrosine can be rapidly and efficiently modified by tetrafluoro-1,4-benzoquinone and other polyhalogenated quinones, which are the major genotoxic and carcinogenic quinoid metabolites of polyhalogenated aromatic compounds. The modification was found to be mainly due to the formation of a variety of fluoroquinone−O-tyrosine conjugates and their hydroxylated derivatives via nucleophilic substitution pathway. Analogous modifications were observed for tyrosine-containing peptides. Further studies showed that the blockade of the reactive phenolic hydroxyl group of tyrosine in the substrate peptide, even by very low concentration of tetrafluoro-1,4-benzoquinone, can prevent the kinase catalyzed tyrosine phosphorylation. This is the first report showing the exceptionally facile chemical modification of the phenolic hydroxyl group of tyrosine by polyhalogenated quinones under normal physiological conditions, which may have potential biological and toxicological implications.

show abstract

“…Our group developed a signal-enhancing system [52,[89][90][91][92] based on the electrocatalytic oxidation of Tyr on indium tin oxide (ITO) electrode, using osmium polypyridine complexes as redox mediators (Scheme 2B). Tyr was chosen as the intrinsic signal reporter due to its lowest oxidation potential of 0.55 V [35] compared with other redox-active AA residues (Table 1).…”

Section: Basic Work: Electrocatalytic Oxidation Of Tyrosinementioning

confidence: 99%

“…We present a range of protein-function analyses in the following section {e.g., monitoring protein-conformation change [52], investigation of protein-ligand interaction [89], detection of oxidative damage of proteins [90], and detection of protein phosphorylation [91,92]}. We also survey and discuss related works involving signal enhancement in these fields.…”

Section: Introductionmentioning

confidence: 99%

Electrocatalytic oxidation of tyrosines shows signal enhancement in label-free protein biosensors

Wei

Famouri

Guo

2012

TrAC Trends in Analytical Chemistry

Self Cite

View full text Add to dashboard Cite

Label-free electrochemical (EC) protein biosensors that derive electrical signal from redox-active amino acid (AA) residues can avoid disruption of delicate protein structures, and thus provide a great opportunity to reveal valid information about protein functions. However, the challenge is that such a signal is usually very limited due to the sluggish EC reaction of free AAs on most common electrodes and slow electron-transfer rates from the deeply-buried AA residues in a protein to the electrode. Signal enhancement therefore becomes crucial. We first survey recent progress in this area.We present a signal-enhancing system that relies on the electrocatalytic oxidation of tyrosine mediated by osmium bipyridine or phenoxazine complexes. We describe several applications of label-free protein EC biosensors based on this detection principle for the analysis of protein functions, including the monitoring of protein-conformation change, study of ligand/protein binding, and detection of protein oxidative damage and protein phosphorylation.We describe related works on protein-function analysis using other signal-enhancing methods. The results suggest that labelfree EC protein biosensors are suitable for the rapid survey of protein functions due to their fast response, ease of integration, cost effectiveness and convenience. Proof-of-concept work on the application of our system is paving the way for bio-analytical detections and protein-function analysis in future work. ª

show abstract

An electrochemical biosensor for the detection of tyrosine oxidation induced by Fenton reaction

Cited by 43 publications

References 27 publications

Development of microplate-based photoelectrochemical DNA biosensor array for high throughput detection of DNA damage

Development of microplate-based photoelectrochemical DNA biosensor array for high throughput detection of DNA damage

The Unexpected and Exceptionally Facile Chemical Modification of the Phenolic Hydroxyl Group of Tyrosine by Polyhalogenated Quinones under Physiological Conditions

Electrocatalytic oxidation of tyrosines shows signal enhancement in label-free protein biosensors

Contact Info

Product

Resources

About