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Spectroscopic and Mechanistic Studies of Dinuclear Metallohydrolases and Their Biomimetic Complexes pp 89–117Cite as

Structural and Mechanistic Studies of Zn(II) Complexes as Phosphoesterase Models

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Part of the book series: Springer Theses ((Springer Theses))

Abstract

Zn(II) is a common metal in all forms of life; it is not only the second most abundant metal in biological systems after iron, but also occurs in the active site of over 200, mostly hydrolytic, enzymes.

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Notes

  1. 1.

    Parts of this chapter have appeared in [L.J. Daumann et al., “Spectroscopic and mechanistic studies of dinuclear metallohydrolases and their biomimetic complexes” Dalton Trans. 2014, 43, 910–928. and L.J. Daumann et al., “The Role of Zn-OR and Zn-OH Nucleophiles and the Influence of p-Substituents in the Reactions of Binuclear Phosphatase Mimetics” Dalton Trans. 2012, 41, 1695–1708.]—Reproduced by permission of The Royal Society of Chemistry.

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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). Structural and Mechanistic Studies of Zn(II) Complexes as Phosphoesterase 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_4

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