caa a22 4500 605507953 CHVBK 20210128100634.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00775-014-1228-0 doi (NATIONALLICENCE)springer-10.1007/s00775-014-1228-0 Recent developments in the study of molybdoenzyme models [Elektronische Daten] [Partha Basu, Sharon Burgmayer] 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. SBIC, 2015 Molybdenum cofactor nationallicence Pyranopterin nationallicence Pterin nationallicence Dithiolene nationallicence Molybdopterin nationallicence Basu Partha Department of Chemistry and Biochemistry, Duquesne University, 15282, Pittsburgh, PA, USA aut Burgmayer Sharon Department of Chemistry, Bryn Mawr College, 19010, Bryn Mawr, PA, USA aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 373-383 0949-8257 20:2<373 2015 20 775 https://doi.org/10.1007/s00775-014-1228-0 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-014-1228-0 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Basu Partha Department of Chemistry and Biochemistry, Duquesne University, 15282, Pittsburgh, PA, USA aut NATIONALLICENCE 700 1- Burgmayer Sharon Department of Chemistry, Bryn Mawr College, 19010, Bryn Mawr, PA, USA aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 373-383 0949-8257 20:2<373 2015 20 775