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Metal Sites in Proteins and Models

Phosphatases, Lewis Acids and Vanadium

  • Book
  • © 1997

Overview

Editors:
  1. H. A. O. Hill
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  2. P. J. Sadler
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  3. A. J. Thomson
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Part of the book series: Springer Desktop Editions in Chemistry (4143)

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Table of contents (6 chapters)

  1. Front Matter

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

    • Eiichi Kimura, Tohru Koike, Mitsuhiko Shionoya
    Pages 1-28

  3. Zinc catalysis in metalloproteases

    • David S. Auld
    Pages 29-50

  4. Modeling the biological chemistry of vanadium: Structural and reactivity studies elucidating biological function

    • Carla Slebodnick, Brent J. Hamstra, Vincent L. Pecoraro
    Pages 51-108

  5. Vanadium bromoperoxidase and functional mimics

    • Alison Butler, Anne H. Baldwin
    Pages 109-132

  6. Metal ions in the mechanism of enzyme-catalysed phosphate monoester hydrolyses

    • David Gani, John Wilkie
    Pages 133-175

  7. The Dimetal Center in purple acid phosphatases

    • Thomas Klabunde, Bernt Krebse
    Pages 177-198

  8. Back Matter

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About this book

Biological chemistry is a major frontier of inorganic chemistry. Three special volumes devoted to Metal Sites in Proteins and Models address the questions: how unusual ("entatic") are metal sites in metalloproteins and metalloenzymes compared to those in small coordination complexes? and if they are special, how do polypeptide chains and co-factors control this? The chapters deal with iron, with metal centres acting as Lewis acids, metals in phosphate enzymes, with vanadium, and with the wide variety of transition metal ions which act as redox centres. They illustrate in particular how the combined armoury of genetics and structure determination at the molecular level are providing unprecedented new tools for molecular engineering.

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