東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

A novel Heme-thiolate peroxygenase A...

Wang, Xiaoshi.

FindBook

Google Book

Amazon

博客來

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

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	A novel Heme-thiolate peroxygenase AaeAPO and its implications for C-H activation chemistry/ by Xiaoshi Wang.
作者:	Wang, Xiaoshi.
出版者:	Cham :Springer International Publishing : : 2016.,
面頁冊數:	xxxii, 130 p. :ill., digital ;24 cm.
內容註:	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
標題:	Heme oxygenase. -
電子資源:	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
LDR:02381nmm a2200325 a 4500 001 2028809
003 DE-He213
005 20160725132117.0
006 m d
007 cr nn 008maaau
008 160908s2016 gw s 0 eng d
020 $a 9783319032368$q(electronic bk.)
020 $a 9783319032351$q(paper)
024 7 $a 10.1007/978-3-319-03236-8 $2 doi
035 $a 978-3-319-03236-8
040 $a GP $c GP
041 0 $a eng
050 4 $a QP603.H45 $b W36 2016
072 7 $a PNN $2 bicssc
072 7 $a SCI013040 $2 bisacsh
082 0 4 $a 547 $2 23
090 $a QP603.H45 $b W246 2016
100 1 $a Wang, Xiaoshi. $3 2179420
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
650 1 4 $a Chemistry. $3 516420
650 2 4 $a Organic Chemistry. $3 890856
650 2 4 $a Enzymology. $3 540241
650 2 4 $a Catalysis. $3 560465
710 2 $a SpringerLink (Online service) $3 836513
773 0 $t Springer eBooks
830 0 $a Springer theses. $3 1314442
856 4 0 $u http://dx.doi.org/10.1007/978-3-319-03236-8
950 $a Chemistry and Materials Science (Springer-11644)