Binary Phosphorene Redox Behavior in Oxidoreductase Enzymatic Systems

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22310%2F19%3A43918147" target="_blank" >RIV/60461373:22310/19:43918147 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216305:26620/19:PU134489

Výsledek na webu

<a href="https://pubs.acs.org/doi/pdf/10.1021/acsnano.9b06230" target="_blank" >https://pubs.acs.org/doi/pdf/10.1021/acsnano.9b06230</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acsnano.9b06230" target="_blank" >10.1021/acsnano.9b06230</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Binary Phosphorene Redox Behavior in Oxidoreductase Enzymatic Systems

Popis výsledku v původním jazyce

Phosphorene is a two-dimensional material that has many advantageous electronic, electrochemical, and optical properties. However, phosphorene possesses a relatively poor stability in ambient atmosphere. This disadvantage limits its application in several systems and particularly in electrochemical biosensors. Here we evaluate phosphorene as an electrochemical biosensing platform in two different mediator-based oxidoreductase enzymatic systems (glucose oxidase (GOx) and peroxidase from horseradish (HRP)), in which their detection is based on the reduction or oxidation of a mediator. In both cases, the used mediator is the same, ferrocene methanol (FcMeOH). Enhanced electrochemical activity is observed only in the reductive system (HRP-based biosensor) when compared to the oxidative counterpart (GOx-based biosensor). This phenomenon is attributed to the fact that in a reductive environment the phosphorene structure remains intact, while in an oxidative potential, the phosphorene is readily oxidized. In this way, the electroactivity of phosphorene as a sensing platform is strongly dependent on the type of mediator-based enzymatic system. These findings of binary nature of phosphorene are of high importance for construction of phosphorene-sensing platforms and in the development of enzyme logic systems. © 2019 American Chemical Society.

Název v anglickém jazyce

Binary Phosphorene Redox Behavior in Oxidoreductase Enzymatic Systems

Popis výsledku anglicky

Phosphorene is a two-dimensional material that has many advantageous electronic, electrochemical, and optical properties. However, phosphorene possesses a relatively poor stability in ambient atmosphere. This disadvantage limits its application in several systems and particularly in electrochemical biosensors. Here we evaluate phosphorene as an electrochemical biosensing platform in two different mediator-based oxidoreductase enzymatic systems (glucose oxidase (GOx) and peroxidase from horseradish (HRP)), in which their detection is based on the reduction or oxidation of a mediator. In both cases, the used mediator is the same, ferrocene methanol (FcMeOH). Enhanced electrochemical activity is observed only in the reductive system (HRP-based biosensor) when compared to the oxidative counterpart (GOx-based biosensor). This phenomenon is attributed to the fact that in a reductive environment the phosphorene structure remains intact, while in an oxidative potential, the phosphorene is readily oxidized. In this way, the electroactivity of phosphorene as a sensing platform is strongly dependent on the type of mediator-based enzymatic system. These findings of binary nature of phosphorene are of high importance for construction of phosphorene-sensing platforms and in the development of enzyme logic systems. © 2019 American Chemical Society.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10402 - Inorganic and nuclear chemistry

Projekt

<a href="/cs/project/GX19-26896X" target="_blank" >GX19-26896X: Elektrochemie 2D Nanomateriálů</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

ACS Nano

ISSN

1936-0851

e-ISSN

—

Svazek periodika

13

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

13217-13224

Kód UT WoS článku

000500650000094

EID výsledku v databázi Scopus

2-s2.0-85073831039