Metal Sites in Proteins and Models

Phosphatases, Lewis Acids and Vanadium
1. Auflage 1997. 2. printing 1999
ISBN: 978-3-540-65553-4
Verlag: Springer Berlin Heidelberg

Buch, Englisch, 198 Seiten, Paperback, Format (B × H): 155 mm x 235 mm, Gewicht: 362 g

Reihe: Springer Desktop Editions in Chemistry

Biological chemistry is a major frontier of inorganic chemistry. Three special volumes devoted to Metal Sites in Proteins andModels 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.

Zielgruppe

Research

Autoren/Hrsg.

Hill, H. A. O.

Thomson, A. J.

Sadler, P.J.

Fachgebiete

• Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Vorklinische Medizin: Grundlagenfächer Molekulare Medizin, Zellbiologie
• Naturwissenschaften Chemie Anorganische Chemie Nichtmetallische Chemie
• Naturwissenschaften Biowissenschaften Angewandte Biologie Biophysik
• Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Klinische und Innere Medizin Immunologie
• Naturwissenschaften Physik Angewandte Physik Biophysik
• Naturwissenschaften Biowissenschaften Enzymologie
• Naturwissenschaften Biowissenschaften Biochemie (nichtmedizinisch)

Inhaltsverzeichnis

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.