Metal sites in proteins and models : redox centres

Bibliographic Information

Metal sites in proteins and models : redox centres

volume editors, H.A.O. Hill, P.J. Sadler, A.J. Thomson ; with contributions by A.F. Arendsen ... [et al.]

(Structure and bonding, 90)

Springer, c1998

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Description and Table of Contents

Description

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.

Table of Contents

Structural characterization of the Mn site in the photosynthetic oxygen-evolving complex.- Metal sites in small blue copper proteins, blue copper oxidases and vanadium-containing enzymes.- Structure and function of the xanthine-oxidase family of molybdenum enzymes.- Nickel-iron hydrogenases: Structural and functional properties.- Coordination sphere versus protein environment as determinants of electronic and functional properties of iron-sulfur proteins.- The bio-inorganic chemistry of tungsten.

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Details
  • NCID
    BA33701059
  • ISBN
    • 3540628886
  • Country Code
    gw
  • Title Language Code
    eng
  • Text Language Code
    eng
  • Place of Publication
    Berlin ; Tokyo
  • Pages/Volumes
    viii, 209 p.
  • Size
    25 cm
  • Parent Bibliography ID
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