Mechanistic Studies of Cd(II) Complexes as Phosphoesterase and Metallo-β-lactamase Models

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Abstract

Cadmium gained its name from the Greek word for kadmeia which is an ancient name for Zn(II) oxide [1]. Cadmium is similar in some ways to Zn(II) and the most common oxidation state is Cd(II). In coordination compounds Cd(II) is often found hepta-coordinate [2, 3]. Cd(II) is often used as a sensor for structural and mechanistic studies of proteins in which Zn(II) is substituted by Cd(II) in their active centers. Often a higher hydrolytic activity is found than in the corresponding Zn(II) enzymes and complexes [2]. This might be due to the increased number of ligands (nucleophiles, substrate) that are possible to bind and exchange at the Cd(II) center. 113Cd NMR spectroscopy is a method used for structure elucidation in biological, inorganic and organometallic cadmium-containing samples [5, 6].

Keywords

Mass Spectrometry Experiment Methyl Parathion Hydrolase Acetate Ligand Terminal Water Terminal Water Molecule 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer International Publishing Switzerland 2014

Authors and Affiliations

  1. 1.School of Chemistry and Molecular BiosciencesUniversity of QueenslandBrisbaneAustralia

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