Scorpionate Complexes as Models for Molybdenum Enzymes. Issue 15 (29th March 2016)

• Record Type: Journal Article
• Authors: Young, Charles G.
• Other Names: Pettinari C. guestEditor.
• Is Part Of: European journal of inorganic chemistry. Issue 15/16(2016)
• Page Start: 2357
• Page End: 2376
• Publication Date: 2016-03-29
• Subjects: Bioinorganic chemistry -- Metalloenzymes -- Enzyme mimics -- Scorpionate complexes -- Molybdenum -- Oxygen atom transfer; Chemistry, Inorganic -- Periodicals; Organometallic chemistry -- Periodicals; Bioinorganic chemistry -- Periodicals; Solid state chemistry -- Periodicals; 546
• DOI: 10.1002/ejic.201501387
• Languages: English
• ISSNs: 1434-1948

Abstract

Abstract : 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. Abstract : The study of molybdenum scorpionate complexes has greatly informed our understanding of the geometric and electronic structures, chemical and spectroscopic properties and mechanisms of action of Mo and W enzymes. This microreview focuses on the biologically relevant oxido‐ and sulfido‐Mo(VI, V, IV) chemistry of hydrotris(R1/2 ‐pyrazolyl)borate and related heteroscorpionate ligands.