Autor: |
Hagen, W. R., Arendsen, A. F., Clarke, M. J., Goodenough, J. B., Jørgensen, C. K., Mingos, D. M. P., Palmer, G. A., Sadler, P. J., Weiss, R., Williams, R. J. P., Hill, H. A. O. |
Zdroj: |
Metal Sites in Proteins & Models Redox Centres; 1998, p161-192, 32p |
Abstrakt: |
Biological chemistry is a major frontier of inorganic chemistry. The three special volumes of Structure and Bonding 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. A steady flow of reports over the last seven years on the molecular characterization of tungsten-containing proteins from a wide range of microorganisms has drastically changed our appreciation of tungsten in redox enzymes. Biological tungsten is not an odd remnant of evolution but a widespread, versatile catalytic entity for the activation of the carbonyl group both in carbon dioxide and in a broad spectrum of aldehydes and carboxylic acids. This review starts off with an outline of the boundary conditions for the biological use of tungsten dictated by inorganic chemistry. Subsequently, the possibilities for spectroscopy on tungsten proteins are reviewed. The molecular properties of tungsten enzymes are described and are related to their physiology and their mechanism of action. Gaps in our current knowledge of the bio-inorganic chemistry of tungsten are identified, and possible directions of future research are indicated. [ABSTRACT FROM AUTHOR] |
Databáze: |
Supplemental Index |
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