Sarah A. Cook , Ethan A. Hill , and A. S. Borovik *
Department of Chemistry, University of California—Irvine, 1102 Natural Sciences II, Irvine, California 92697, United States
Biochemistry, Article ASAP
DOI: 10.1021/acs.biochem.5b00249
Publication Date (Web): June 16, 2015
Copyright © 2015 American Chemical Society
*E-mail: aborovik@uci.edu. Phone: (949) 824-1510.
Abstract
Metalloproteins
contain actives sites with intricate structures that perform specific
functions with high selectivity and efficiency. The complexity of these
systems complicates the study of their function and the understanding of
the properties that give rise to their reactivity. One approach that
has contributed to the current level of understanding of their
biological function is the study of synthetic constructs that mimic one
or more aspects of the native metalloproteins. These systems allow
individual contributions to the structure and function to be analyzed
and also permit spectroscopic characterization of the metal cofactors
without complications from the protein environment. This Current Topic
is a review of synthetic constructs as probes for understanding the
biological activation of small molecules. These topics are developed
from the perspective of seminal molecular design breakthroughs from the
past that provide the foundation for the systems used today.
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