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A novel Heme-thiolate peroxygenase A...

Wang, Xiaoshi.

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A novel Heme-thiolate peroxygenase AaeAPO and its implications for C-H activation chemistry

Record Type:	Electronic resources : Monograph/item
Title/Author:	A novel Heme-thiolate peroxygenase AaeAPO and its implications for C-H activation chemistry/ by Xiaoshi Wang.
Author:	Wang, Xiaoshi.
Published:	Cham :Springer International Publishing : : 2016.,
Description:	xxxii, 130 p. :ill., digital ;24 cm.
[NT 15003449]:	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.
Contained By:	Springer eBooks
Subject:	Heme oxygenase. -
Online resource:	http://dx.doi.org/10.1007/978-3-319-03236-8
ISBN:	9783319032368$q(electronic bk.)

A novel Heme-thiolate peroxygenase AaeAPO and its implications for C-H activation chemistry
Wang, Xiaoshi.

A novel Heme-thiolate peroxygenase AaeAPO and its implications for C-H activation chemistry[electronic resource] /by Xiaoshi Wang. - Cham :Springer International Publishing :2016. - xxxii, 130 p. :ill., digital ;24 cm. - Springer theses,2190-5053. - Springer theses..

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.

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.

ISBN: 9783319032368$q(electronic bk.)

Standard No.: 10.1007/978-3-319-03236-8doiSubjects--Topical Terms:

2179421
Heme oxygenase.

LC Class. No.: QP603.H45 / W36 2016

Dewey Class. No.: 547

A novel Heme-thiolate peroxygenase AaeAPO and its implications for C-H activation chemistry
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245 1 2 $a A novel Heme-thiolate peroxygenase AaeAPO and its implications for C-H activation chemistry $h [electronic resource] / $c by Xiaoshi Wang.
260 $a Cham : $b Springer International Publishing : $b Imprint: Springer, $c 2016.
300 $a xxxii, 130 p. : $b ill., digital ; $c 24 cm.
490 1 $a Springer theses, $x 2190-5053
505 0 $a 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.
520 $a 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.
650 0 $a Heme oxygenase. $3 2179421
650 0 $a Hydroxylation. $3 2179422
650 0 $a Alkanes. $3 871058
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650 2 4 $a Enzymology. $3 540241
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856 4 0 $u http://dx.doi.org/10.1007/978-3-319-03236-8
950 $a Chemistry and Materials Science (Springer-11644)