Characterization of metal binding sites in fulvic acids by lanthanide ion probe spectroscopy

1989 ◽  
Vol 61 (5) ◽  
pp. 483-488 ◽  
Author(s):  
J. C. Dobbs ◽  
W. Susetyo ◽  
F. E. Knight ◽  
M. A. Castles ◽  
Lionel A. Carreira ◽  
...  
1996 ◽  
Vol 50 (3) ◽  
pp. 401-408 ◽  
Author(s):  
J. W. Thomason ◽  
W. Susetyo ◽  
L. A. Carreira

The acidic functional groups of humic materials are an abundant source of metal binding sites in the natural environment. Studies of metal binding to humics are of great environmental interest because the biological and physicochemical properties of metals are often changed dramatically as a result of complexation with humics. In order to understand how these heterogeneous organic macromolecules bind metals with such a large range of binding energies, lanthanide ion probe spectroscopy (LIPS) has been used to study changes in the fluorescence lifetime of the europium probe metal as it binds to these substances. A method developed by Horrocks and Sudnick for the determination of the number of water molecules bound to Eu3+ was used to calculate the coordination number of humic-bound Eu3+ from the fluorescence data. The peak shift of the Eu3+ hypersensitive emission band (616 nm) was used to calculate the change in charge of the complex. Equations based on Horrocks and Sudnick's method were also developed to calculate the distribution of metal associated with the different types of binding sites on humic substances by computer modeling of the fluorescence lifetime data.


Metallomics ◽  
2017 ◽  
Vol 9 (11) ◽  
pp. 1534-1547 ◽  
Author(s):  
Irene Russo Krauss ◽  
Giarita Ferraro ◽  
Andrea Pica ◽  
José A. Márquez ◽  
John R. Helliwell ◽  
...  

Examples from the literature and experience in our own laboratory on the characterization of the interactions between biological macromolecules and metal-based drugs are provided.


2015 ◽  
Vol 472 (2) ◽  
pp. 205-216 ◽  
Author(s):  
Isabelle Petit-Härtlein ◽  
Kevin Rome ◽  
Eve de Rosny ◽  
Florian Molton ◽  
Carole Duboc ◽  
...  

ZraP is an octamer containing four interfacial metal-binding sites contributing to dimer stability. Zinc binding enhances its chaperone properties and zinc-bound ZraP represses the expression of the zraPSR operon. None of the Zra proteins are involved in zinc resistance.


RSC Advances ◽  
2020 ◽  
Vol 10 (63) ◽  
pp. 38612-38616
Author(s):  
Djawed Nauroozi ◽  
Benjamin Wurster ◽  
Rüdiger Faust

Synthesis and structural characterization of a geminal enediyne molecule with three imine metal binding sites based on diazafluorenemethylidene in a cross-π-conjugated fashion is reported.


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