Bibliographic Information

Iron centres

H.A.O. Hill, P.J. Sadler, A.J. Thomson (eds.)

(Springer desktop editions in chemistry, . Metal sites in proteins and models)

New York : Springer-Verlag, 1999

Available at  / 11 libraries

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Note

Includes bibliographical references and index

"This is the first of 3 special volumes of Structure and bonding (volumes 88, 89, and 90)"--Pref

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

Polyiron oxides, oxyhydroxides and hydroxides as models for biomineralisation processes.- Heme: The most versatile redox centre in biology?.- Rationalisation of metal binding to transferrin: Prediction of metal-protein stability constants.- Metal centres of bacterioferritins or non-haem-iron-containing cytochromes b 557.- Ribonucleotide reductases - a group of enzymes with different metallosites and a similar reaction mechanism.- Protein engineering of cytochrome P450cam.

by "Nielsen BookData"

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Details

  • NCID
    BA42253017
  • ISBN
    • 3540655522
  • LCCN
    99020162
  • Country Code
    gw
  • Title Language Code
    eng
  • Text Language Code
    eng
  • Place of Publication
    Berlin
  • Pages/Volumes
    207 p.
  • Size
    24 cm
  • Classification
  • Subject Headings
  • Parent Bibliography ID
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