Originally published as volume 88 in the series: Structure and Bonding
VII, 207 p.
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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.
Polyiron oxides, oxyhydroxides and hydroxides as models for biomineralisation processes.- Heme: The most versatile redox centre in biology?.- Rationalisation of metal binding to transferrin: Prediction of metal-protein stability constants.- Metal centres of bacterioferritins or non-haem-iron-containing cytochromes b 557.- Ribonucleotide reductases — a group of enzymes with different metallosites and a similar reaction mechanism.- Protein engineering of cytochrome P450cam.