Abstract
The control of the catalytic properties of metal ions in enzymes is discussed through three illustrations: the zinc enzymes carbonic anhydrase, carboxypeptidase, and alcohol dehydrogenase. They represent examples of the variation in reactivity of zinc ions placed in different biological environments leading to well-defined molecular species with different catalytic functions. Two levels of speciation are discussed:
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1)
basic chemical characteristics of a species by choice of the number, the chemical nature and geometric arrangement of protein side chains binding the metal; and
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2)
modulation of the metal species reactivity by structural changes induced by substrate and/or coenzyme binding which, inter alia, may alter the geometry, accessibility, and polarity of the functional metal-binding site.
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© 1986 Dr. S. Bernhard, Dahlem Konferenzen
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Zeppezauer, M., Maret, W. (1986). Does the Coordination Environment Determine the Reactivity of Metals in Enzymes?. In: Bernhard, M., Brinckman, F.E., Sadler, P.J. (eds) The Importance of Chemical “Speciation” in Environmental Processes. Dahlem Workshop Reports, vol 33. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70441-3_8
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DOI: https://doi.org/10.1007/978-3-642-70441-3_8
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