Metal Sites in Proteins and Models
Metal Sites in Proteins and Models
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.
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.
Advances in Zinc Enzyme Models by Small, Mononuclear Zinc (II) Complexes
Zinc catalysis in metalloproteasesModeling 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.
Hill, H. A. O.
Sadler, P. J.
Thomson, A. J.
ISBN | 978-3-540-65553-4 |
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Artikelnummer | 9783540655534 |
Medientyp | Buch |
Copyrightjahr | 1999 |
Verlag | Springer, Berlin |
Umfang | VII, 198 Seiten |
Abbildungen | VII, 198 p. 134 illus., 13 illus. in color. |
Sprache | Englisch |