Metal Sites In Proteins And Models: Phosphatases, Lewis Acids And Vanadium (structure And Bonding) (vol 89)

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. Covers the dimetal center in purple acid phosphatases, vanadium bromoperoxidase & functional mimics, etc. Advances in Zinc Enzyme Models by Small, Mononuclear Zinc (II) Complexes....Pages 1-28 Zinc catalysis in metalloproteases....Pages 29-50 Modeling the biological chemistry of vanadium: Structural and reactivity studies elucidating biological function....Pages 51-108 Vanadium bromoperoxidase and functional mimics....Pages 109-132 Metal ions in the mechanism of enzyme-catalysed phosphate monoester hydrolyses....Pages 133-175 The Dimetal Center in purple acid phosphatases....Pages 177-198 The first in a three-volume set which presents the results of recent research in the field of metalloproteins and models. It deals with iron, metal centres acting as Lewis acids, metals in phosphate enzymes, vanadium and the wide variety of transition metal ions acting as redox centres. The last in a three-volume set which presents the results of recent research in the field of metalloproteins and models. It deals with iron, metal centres acting as Lewis acids, metals in phosphate enzymes, vanadium and the wide variety of transition metal ions acting as redox centres.