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Spectroscopic and Mechanistic Studies of Dinuclear Metallohydrolases and Their Biomimetic Complexes pp 119–143Cite as

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].

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Notes

  1. 1.

    Parts of this Chapter have been reprinted with permission from (L.J. Daumann et al., "Cadmium(II) Complexes: Mimics of Organophosphate Pesticide Degrading Enzymes and Metallo-β-lactamases" Inorg. Chem. 2012, 51, 7669–7681). Copyright (2014) American Chemical Society.

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  1. School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, QLD, Australia

    Lena Josefine Daumann

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Daumann, L.J. (2014). Mechanistic Studies of Cd(II) Complexes as Phosphoesterase and Metallo-β-lactamase Models. In: Spectroscopic and Mechanistic Studies of Dinuclear Metallohydrolases and Their Biomimetic Complexes. Springer Theses. Springer, Cham. https://doi.org/10.1007/978-3-319-06629-5_5

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