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Record Nr. |
UNINA990001706820403321 |
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Autore |
Ravaz, L. |
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Titolo |
Les vignes americaines : porte-greffes et producteurs-directs / L. Ravaz |
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Pubbl/distr/stampa |
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Montpellier, : Coulet, 1902 |
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Descrizione fisica |
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Disciplina |
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Locazione |
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Collocazione |
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60 634.84 B 2 |
A MUSA 1044 |
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Lingua di pubblicazione |
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Formato |
Materiale a stampa |
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Livello bibliografico |
Monografia |
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2. |
Record Nr. |
UNINA9910254057303321 |
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Autore |
Wang Xiaoshi |
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Titolo |
A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry / / by Xiaoshi Wang |
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Pubbl/distr/stampa |
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Cham : , : Springer International Publishing : , : Imprint : Springer, , 2016 |
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ISBN |
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Edizione |
[1st ed. 2016.] |
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Descrizione fisica |
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1 online resource (153 p.) |
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Collana |
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Springer Theses, Recognizing Outstanding Ph.D. Research, , 2190-5053 |
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Disciplina |
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Soggetti |
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Chemistry, Organic |
Enzymology |
Catalysis |
Organic Chemistry |
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Lingua di pubblicazione |
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Formato |
Materiale a stampa |
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Livello bibliografico |
Monografia |
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Note generali |
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Description based upon print version of record. |
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Nota di bibliografia |
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Includes bibliographical references at the end of each chapters. |
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Nota di contenuto |
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From 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. |
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Sommario/riassunto |
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In 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. |
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