Metal Sites in Proteins and Models
Phosphatases, Lewis Acids and Vanadium
Springer (Publisher)
1st Edition
Published on 4. September 1997
Book
Hardback
VII, 198 pages
978-3-540-62874-3 (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
Language
English
Place of publication
Heidelberg
Germany
Publishing group
Springer Berlin
Target group
Professional and scholarly
Research
Illustrations
13 farbige Abbildungen, 13 s/w Tabellen, 121 s/w Abbildungen
12 colour figures, 82 b&w figures, 13 tables
Dimensions
Height: 23.5 cm
Width: 15.5 cm
Weight
475 gr
ISBN-13
978-3-540-62874-3 (9783540628743)
DOI
10.1007/3-540-62874-6
Schweitzer Classification
Other editions
Additional editions

H.A.O. Hill | P.J. Sadler | A.J. Thomson
Metal Sites in Proteins and Models
Phosphatases, Lewis Acids and Vanadium
E-Book
07/2005
Springer
€53.49
Available for download

H.A.O. Hill | P.J. Sadler | A.J. Thomson
Metal Sites in Proteins and Models
Phosphatases, Lewis Acids and Vanadium
Book
04/1999
Springer
€53.49
Shipment within 7-9 days
Content
Advances in Zinc Enzyme Models by Small, Mononuclear Zinc (II) Complexes.- Zinc catalysis in metalloproteases.- Modeling the biological chemistry of vanadium: Structural and reactivity studies elucidating biological function.- Vanadium bromoperoxidase and functional mimics.- Metal ions in the mechanism of enzyme-catalysed phosphate monoester hydrolyses.- The Dimetal Center in purple acid phosphatases.