
Metal Sites in Proteins and Models
Redox Centres
Springer (Publisher)
Published on 1. April 1999
Book
Paperback/Softback
XI, 209 pages
978-3-540-65556-5 (ISBN)
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.
More details
Series
Edition
1st ed. 1998. 2nd printing
Language
English
Place of publication
Berlin
Germany
Publishing group
Springer Berlin
Target group
College/higher education
Professional and scholarly
Research
Illustrations
5 s/w Abbildungen, 33 farbige Abbildungen
XI, 209 p. 38 illus., 33 illus. in color.
Dimensions
Height: 23.5 cm
Width: 15.5 cm
Weight
349 gr
ISBN-13
978-3-540-65556-5 (9783540655565)
DOI
10.1007/3-540-62888-6
Schweitzer Classification
Other editions
Additional editions

E-Book
07/2006
Springer
€149.79
Available for download

Book
11/1997
Springer
€160.49
Article exhausted; check different version
Content
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.