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Lena Daumanns's thesis describes structural and functional studies of the enzyme Glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes. It also examines the properties of small mimics of this enzyme and related binuclear metallohydrolases such as the metallo-ß-lactamases to enhance our understanding of hydrolytic cleavage of important substrates like phosphoesters and beta-lactams. Overall, this project has led to a better understanding of the metal ion binding and active site structural features of the enzyme GpdQ. Daumann describes how she successfully immobilized phosphoesterase and related biomimetics on solid supports for potential applications in the area of bioremediation of organophosphate pesticides. Analysis shows that both the enzyme and biomimetics can be stored on the solid support without loss of activity. Furthermore, the author specroscopically and mechanistically characterized a number of Zn(II), Cd(II) and Co(II) complexes, some of which are among the most active biomimetics towards organophosphates reported to date. This thesis makes excellent reading for non-specialists because each chapter includes a short introduction section.
List of contents
Introduction.- Experimental.- Understanding the Overall Structure of GpdQ and Metal Binding.- Structural and Mechanistic Studies of Zn(II) Complexes as Phosphoesterase Models.- Mechanistic Studies of Cd(II) Complexes as Phosphoesterase and Metallo-beta-lactamase Models.- Spectroscopic and Mechanistic Studies of Co(II) Phosphoesterase and Metallo-beta-lactamase Biomimetics.- Asymmetric Zn(II) Complexes as Structural and Functional Models for GpdQ.- Immobilization of GpdQ and Related Models for Bioremedial Applications.- Conclusion and Outlook.
About the author
Lena Daumann holds a Diploma in Chemistry from the University of Heidelberg, Germany, where she worked with Professor Peter Comba. After gathering six months industrial experience at the BASF chemical company, she commenced her PhD in 2010 at the University of Queensland, Australia, under the supervision of Professor Lawrence Gahan. She received her doctoral degree in 2013 in the field of Bioinorganic Chemistry and currently holds a position as a postdoctoral researcher at the University of California, Berkeley, in the group of Professor Kenneth Raymond, funded by a fellowship of the Humboldt Foundation.
Summary
Lena Daumanns's thesis describes structural and functional studies of the enzyme Glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes. It also examines the properties of small mimics of this enzyme and related binuclear metallohydrolases such as the metallo-ß-lactamases to enhance our understanding of hydrolytic cleavage of important substrates like phosphoesters and β-lactams. Overall, this project has led to a better understanding of the metal ion binding and active site structural features of the enzyme GpdQ. Daumann describes how she successfully immobilized phosphoesterase and related biomimetics on solid supports for potential applications in the area of bioremediation of organophosphate pesticides. Analysis shows that both the enzyme and biomimetics can be stored on the solid support without loss of activity. Furthermore, the author specroscopically and mechanistically characterized a number of Zn(II), Cd(II) and Co(II) complexes, some of which are among the most active biomimetics towards organophosphates reported to date. This thesis makes excellent reading for non-specialists because each chapter includes a short introduction section.
