Novel determination of cadmium ions using an enzyme self-assembled monolayer with surface plasmon resonance

May May, L and Russell, David (2003) Novel determination of cadmium ions using an enzyme self-assembled monolayer with surface plasmon resonance. Analytica Chimica Acta, 500 (1-2). pp. 119-125. ISSN 1873-4324

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Abstract

The activity of the enzyme urease is known to be inhibited by the heavy metal cadmium. The binding of cadmium to urease and the consequent changes of the enzyme structure are the basis of the surface plasmon resonance (SPR) biosensing system reported herein. To facilitate the formation of a self-assembled monolayer (SAM) of the urease on gold-coated glass SPR sensor disks, the enzyme has been modified with N-succinimidyl 3-(2-pyridyldithiol) propionate (SPDP). The urease monolayer was exposed to trace levels of cadmium ions and monitored by SPR. From circular dichroism (CD) data, it is believed that the conformation of the active nickel site of the urease changes upon binding of the cadmium ions. It is this change of the enzyme monolayer, measured by SPR, which has been related to the cadmium ion concentration in the range of 0–10 mg l-1. These data are the first report of a SPR biosensor capable of detecting metal ions.

Item Type: Article
Faculty \ School: Faculty of Science > School of Chemistry
Related URLs:
Depositing User: Rachel Smith
Date Deposited: 21 Jan 2011 16:45
Last Modified: 24 Jul 2019 17:03
URI: https://ueaeprints.uea.ac.uk/id/eprint/19737
DOI: 10.1016/S0003-2670(03)00943-7

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