Recent Developments in the Study of Molybdoenzyme Models
Document Type
Article
Version
Final Published Version
Publication Title
Journal of Biological Inorganic Chemistr
Volume
20
Publication Date
2015
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.
Citation
Basu, Partha, and Sharon J. Nieter Burgmayer. 2015. “Recent Developments in the Study of Molybdoenzyme Models.” Journal of Biological Inorganic Chemistry 20 (2): 373–83. https://doi.org/10.1007/s00775-014-1228-0.
DOI
https://doi.org/10.1007/s00775-014-1228-0