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Scorpionate Complexes as Models for Molybdenum Enzymes
Author(s) -
Young Charles G.
Publication year - 2016
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.201501387
Subject(s) - chemistry , molybdenum , pterin , sulfur , combinatorial chemistry , electron transfer , catalysis , enzyme , bioinorganic chemistry , metal , stereochemistry , organic chemistry , cofactor
Scorpionate ligands have supported the development of a number of important synthetic models for pterin‐containing molybdenum enzymes. These ligands stabilize biologically relevant mononuclear oxido‐ and sulfido‐Mo(VI,V,IV) complexes capable of sustaining a wide range of biomimetic reactions, including oxygen atom, sulfur atom and coupled electron‐proton transfer reactions. Studies of scorpionate‐Mo compounds have also provided key insights into the bonding in oxido‐Mo dithiolene moieties, the orbital control of enzymatic reactions and the synthesis and behavior of biologically relevant Mo‐pterindithiolene complexes. This microreview covers advances in the synthesis and study of scorpionate complexes as models for molybdenum enzymes in the second half of the field's 30‐year history, i.e., from around 2000, the turn of the century, onwards.