Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

    We have a manual that explains all the features 

Record number 555424
Title Stripping chronopotentiometry at scanned deposition potential (SSCP) : An effective methodology for dynamic speciation analysis of nanoparticulate metal complexes
Author(s) Town, Raewyn M.; Leeuwen, Herman P. van
Source Journal of Electroanalytical Chemistry 853 (2019). - ISSN 1572-6657
Department(s) Physical Chemistry and Soft Matter
Publication type Refereed Article in a scientific journal
Publication year 2019
Keyword(s) Chemical heterogeneity - Dynamic metal speciation - Humic substances - Lability - Nanoparticulate complexants

The features of stripping chronopotentiometry at scanned deposition potential (SSCP) are reviewed and placed in context with voltammetric and other dynamic speciation techniques. The advantages of SSCP for speciation analysis of nanoparticulate metal complexes are highlighted. Analogous to other electrochemical techniques, the SSCP wave is rich in information: the measurements from the foot to the plateau of the wave access the relevant parts of the stability distribution and the rate constant distributions. The complete depletion regime of SSCP offers particular advantages due to its ability to unambiguously distinguish between various factors that can confound interpretation of data from other electroanalytical methods, including electrochemical irreversibility, kinetically controlled currents, reduced diffusion coefficient of the metal complex species as compared to the free metal ion, and chemical heterogeneity in the intrinsic binding affinity.

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