LEADER 03698nam 22006615 450 001 9910254057303321 005 20200704115054.0 010 $a3-319-03236-4 024 7 $a10.1007/978-3-319-03236-8 035 $a(CKB)3710000000492496 035 $a(EBL)4178146 035 $a(SSID)ssj0001584172 035 $a(PQKBManifestationID)16264569 035 $a(PQKBTitleCode)TC0001584172 035 $a(PQKBWorkID)14864741 035 $a(PQKB)11791328 035 $a(DE-He213)978-3-319-03236-8 035 $a(MiAaPQ)EBC4178146 035 $a(PPN)190536756 035 $a(EXLCZ)993710000000492496 100 $a20151016d2016 u| 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 12$aA Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry /$fby Xiaoshi Wang 205 $a1st ed. 2016. 210 1$aCham :$cSpringer International Publishing :$cImprint: Springer,$d2016. 215 $a1 online resource (153 p.) 225 1 $aSpringer Theses, Recognizing Outstanding Ph.D. Research,$x2190-5053 300 $aDescription based upon print version of record. 311 $a3-319-03235-6 320 $aIncludes bibliographical references at the end of each chapters. 327 $aFrom the Contents: Hydrocarbon Oxygenation by Heme-Thiolate Enzymes -- Efficient and Selective Alkane Hydroxylation Reactions Catalyzed by the Fungal Peroxygenase AaeAPO -- Hydrocarbon Hydroxylations Catalyzed by AaeAPO: Evidence of Radical Intermediates and Kinetic Isotope Effects. 330 $aIn this thesis, Xiaoshi Wang investigates the function and mechanism of a newly discovered heme-thiolate peroxygenase, AaeAPO. This enzyme class comes from Agrocybe aegerita and is used in the conversion of inert hydrocarbons to alcohols. Xiaoshi's work focuses on an extracellular P450 enzyme which is not limited in its stability and lack of solubility and therefore is relevant for widespread industrial use. The author demonstrates that the peroxygenase catalyzes a wide range of reactions. In some cases the author even describes very difficult transformations in molecules that are highly inert. Her detailed investigations provide a mechanistic framework for how the peroxygenase catalyzes such a large number of reactions. A major highlight of this thesis is the identification of key short-lived intermediates in the catalytic cycle of the peroxygenase, using rapid kinetic and spectroscopic methods, as well as the elucidation of the thermodynamic properties of these high-energy intermediates. This work adds new insight into an important class of enzymes. 410 0$aSpringer Theses, Recognizing Outstanding Ph.D. Research,$x2190-5053 606 $aChemistry, Organic 606 $aEnzymology 606 $aCatalysis 606 $aOrganic Chemistry$3https://scigraph.springernature.com/ontologies/product-market-codes/C19007 606 $aEnzymology$3https://scigraph.springernature.com/ontologies/product-market-codes/L14070 606 $aCatalysis$3https://scigraph.springernature.com/ontologies/product-market-codes/C29000 615 0$aChemistry, Organic. 615 0$aEnzymology. 615 0$aCatalysis. 615 14$aOrganic Chemistry. 615 24$aEnzymology. 615 24$aCatalysis. 676 $a612.1111 700 $aWang$b Xiaoshi$4aut$4http://id.loc.gov/vocabulary/relators/aut$01061405 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910254057303321 996 $aA Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry$92518743 997 $aUNINA