Abstract
Catalysis by metalloenzymes occupies a relatively unique position when placed in a general consideration of heterogeneous and homogeneous catalysis. The distinguishing feature of course is that even if one tends to focus on the metal ion as essential to the catalytic center, one must remember that this center carries with it a large protein molecule of molecular weight from 6000 in the simplest cases to over a 100 000 in the more complex metalloenzymes. The primary, secondary, and tertiary structure of the macromolecule surrounding the metal ion, resulting from the folding of the amino-acid polymer (and believed to be dictated by the primary sequence of the 20 different amino acids), makes possible an enormous variation in the microenvironment of the metal ion. This microenvironment can also determine the reactivity of the organic groups (the various amino-acid side-chains) that can assume a role in a given catalytic reaction in addition to the metal ion. Such variation is not readily achieved in small molecular systems. Since the great specificity and enormous rate enhancements at 37°C characteristic of biological catalysis are a property of catalytically active protein molecules, many of which do not contain metal ions, the chemistry of metalloenzymes must be considered as a special case of enzymatic catalysis.
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Coleman, J.E. (1973). Catalysis by Metalloenzymes. In: Basolo, F., Burwell, R.L. (eds) Catalysis Progress in Research. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-4577-0_2
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DOI: https://doi.org/10.1007/978-1-4613-4577-0_2
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