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Advances in Zinc Enzyme Models by Small, Mononuclear Zinc (II) Complexes

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Metal Sites in Proteins and Models

Part of the book series: Structure and Bonding ((4143,volume 89))

Abstract

Recent developments in zinc enzyme models, in particular for carbonic anhydrase (CA), alkaline phosphatase (AP), and alcohol dehydrogenase (ADH) are presented. Although these models are simple zinc(II) complexes, they have helped to disclose the hitherto unsettled intrinsic properties of zinc (II)-dependent enzyme functions. The discussion emphasizes how H2O is activated by zinc(II) for the nucleophilic attack on electrophilic substrates (e.g., CO2 in CA, phosphomonoesters in AP) and also how alcohols are activated by zinc (II) for hydride transfer in ADH or nucleophilic attack on phosphates in AP. Future modeling should take into consideration the results from recent developments in enzyme functions by protein engineering. For instance, design of secondary zinc(II) ligands for the fine-tuning of zinc(II) properties will be needed to explore and understand the reaction specificity of zinc enzymes.

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Authors and Affiliations

  1. Department of Medicinal Chemistry, School of Medicine, Hiroshima University, Kasumi, 1-2-3, Minami-ku, 734, Hiroshima, Japan

    Eiichi Kimura & Tohru Koike

  2. Institute for Molecular Science, Okazaki National Institutes, Nishigonaka 38, 444, Myodaij, Okazaki, Japan

    Mitsuhiko Shionoya

Authors
  1. Eiichi Kimura
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  2. Tohru Koike
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  3. Mitsuhiko Shionoya
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Editor information

H. A. O. Hill P. J. Sadler A. J. Thomson

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© 1997 Springer Verlag

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Kimura, E., Koike, T., Shionoya, M. (1997). Advances in Zinc Enzyme Models by Small, Mononuclear Zinc (II) Complexes. In: Hill, H.A.O., Sadler, P.J., Thomson, A.J. (eds) Metal Sites in Proteins and Models. Structure and Bonding, vol 89. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-62874-6_7

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  • DOI: https://doi.org/10.1007/3-540-62874-6_7

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  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-62874-3

  • Online ISBN: 978-3-540-69037-5

  • eBook Packages: Springer Book Archive

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