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Science 12 March 1993:
Vol. 259. no. 5101, pp. 1575 - 1581
DOI: 10.1126/science.8384374
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Articles

Science, Vol 259, Issue 5101, 1575-1581
Copyright © 1993 by American Association for the Advancement of Science

articles

Electronic structure contributions to function in bioinorganic chemistry

EI Solomon and MD Lowery

Department of Chemistry, Stanford University, CA 94305.

Many metalloenzymes exhibit distinctive spectral features that are now becoming well understood. These reflect active site electronic structures that can make significant contributions to catalysis. Copper proteins provide well-characterized examples in which the unusual electronic structures of their active sites contribute to rapid, long-range electron transfer reactivity, oxygen binding and activation, and the multielectron reduction of dioxygen to water.


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Evidence of the Indirect Formation of the Catecholic Intermediate Substrate Responsible for the Autoactivation Kinetics of Tyrosinase.
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Metalloenzymes, structural motifs, and inorganic models.
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