title: Recent developments in the study of molybdoenzyme models.
abstract: Over the past two decades, a plethora of crystal structures of molybdenum enzymes has appeared in the literature providing a clearer picture of the enzymatic active sites and increasing the challenge to chemists to develop accurate models for those sites. In this minireview we discuss the most recent model studies aimed to reproduce detailed features of the pterin-dithiolene ligand, both as the uncoordinated form and as a chelate coordinated to molybdenum.
authors.affiliation: Department of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA, 15282, USA, basu@duq.edu.
authors.forename: Partha
authors.initials: P
authors.lastname: Basu
authors.forename: Sharon J Nieter
authors.initials: SJ
authors.lastname: Burgmayer
mesh_terms: D001665:Binding Sites; D020134:Catalytic Domain; D003067:Coenzymes / Q000737:chemistry*; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008024:Ligands; D015394:Molecular Structure; D008982:Molybdenum / Q000737:chemistry*; D011621:Pteridines / Q000737:chemistry; D011622:Pterins / Q000737:chemistry
chemical_list: D003067:Coenzymes; D007506:Iron-Sulfur Proteins; D008024:Ligands; D011621:Pteridines; D011622:Pterins; D008982:Molybdenum