LEADER 04245nam 22006735 450 001 9910298654003321 005 20200702172604.0 010 $a3-319-06629-3 024 7 $a10.1007/978-3-319-06629-5 035 $a(CKB)3710000000119133 035 $a(EBL)1731135 035 $a(OCoLC)884585517 035 $a(SSID)ssj0001237479 035 $a(PQKBManifestationID)11735475 035 $a(PQKBTitleCode)TC0001237479 035 $a(PQKBWorkID)11259023 035 $a(PQKB)10811285 035 $a(MiAaPQ)EBC1731135 035 $a(DE-He213)978-3-319-06629-5 035 $a(PPN)178785415 035 $a(EXLCZ)993710000000119133 100 $a20140528d2014 u| 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 10$aSpectroscopic and Mechanistic Studies of Dinuclear Metallohydrolases and Their Biomimetic Complexes$b[electronic resource] /$fby Lena Josefine Daumann 205 $a1st ed. 2014. 210 1$aCham :$cSpringer International Publishing :$cImprint: Springer,$d2014. 215 $a1 online resource (253 p.) 225 1 $aSpringer Theses, Recognizing Outstanding Ph.D. Research,$x2190-5053 300 $a"Doctoral Thesis accepted by University of Queensland, Australia." 311 $a3-319-06628-5 320 $aIncludes bibliographical references at the end of each chapters. 327 $aIntroduction -- 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-?-lactamase Models -- Spectroscopic and Mechanistic Studies of Co(II) Phosphoesterase and Metallo-?-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. 330 $aLena Daumanns's thesis describes structural and functional studies of the enzyme Glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes. It also examines the properties of small mimics of this enzyme and related binuclear metallohydrolases such as the metallo-ß-lactamases to enhance our understanding of hydrolytic cleavage of important substrates like phosphoesters and ?-lactams. Overall, this project has led to a better understanding of the metal ion binding and active site structural features of the enzyme GpdQ. Daumann describes how she successfully immobilized phosphoesterase and related biomimetics on solid supports for potential applications in the area of bioremediation of organophosphate pesticides. Analysis shows that both the enzyme and biomimetics can be stored on the solid support without loss of activity. Furthermore, the author specroscopically and mechanistically characterized a number of Zn(II), Cd(II) and Co(II) complexes, some of which are among the most active biomimetics towards organophosphates reported to date. This thesis makes excellent reading for non-specialists because each chapter includes a short introduction section. 410 0$aSpringer Theses, Recognizing Outstanding Ph.D. Research,$x2190-5053 606 $aBiochemical engineering 606 $aEnzymology 606 $aSpectroscopy 606 $aBiochemical Engineering$3https://scigraph.springernature.com/ontologies/product-market-codes/C12029 606 $aEnzymology$3https://scigraph.springernature.com/ontologies/product-market-codes/L14070 606 $aSpectroscopy/Spectrometry$3https://scigraph.springernature.com/ontologies/product-market-codes/C11020 615 0$aBiochemical engineering. 615 0$aEnzymology. 615 0$aSpectroscopy. 615 14$aBiochemical Engineering. 615 24$aEnzymology. 615 24$aSpectroscopy/Spectrometry. 676 $a574.19296 700 $aDaumann$b Lena Josefine$4aut$4http://id.loc.gov/vocabulary/relators/aut$01061775 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910298654003321 996 $aSpectroscopic and Mechanistic Studies of Dinuclear Metallohydrolases and Their Biomimetic Complexes$92520037 997 $aUNINA