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Structural studies on extradiol diox...

Koksal, Mustafa.

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Structural studies on extradiol dioxygenases: Strategies for improved bioremediation of PCBs.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Structural studies on extradiol dioxygenases: Strategies for improved bioremediation of PCBs./
Author:	Koksal, Mustafa.
Description:	240 p.
Notes:	Adviser: Jeffrey T. Bolin.
Contained By:	Dissertation Abstracts International68-12B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3291071
ISBN:	9780549357551

Structural studies on extradiol dioxygenases: Strategies for improved bioremediation of PCBs.
Koksal, Mustafa.

Structural studies on extradiol dioxygenases: Strategies for improved bioremediation of PCBs. - 240 p.

Adviser: Jeffrey T. Bolin.

Thesis (Ph.D.)--Purdue University, 2007.

Bioremediation has emerged as a possible alternative to other non-biological methods to eliminate polychlorinated biphenyls (PCBs). However, there are limitations due to inabilities of the microorganisms that may be used in this process. 2,3-dihydroxybiphenyl-1,2-dioxygenase (DHBD), which cleaves the aromatic ring of PCBs, is one of the key enzymes in the biodegradation pathway, determining the ability of an organism to degrade a wide variety of PCBs. Burkholderia xenovorans strain LB400 is a potential candidate organism for bioremediation applications, however, DHBDLB400 suffers from substrate-facilitated suicide inactivation, poor catalytic activity and low substrate specificity for some PCB congeners. Supplementation of the organism with DHBD variants from other pathways was considered as a powerful strategy to improve the capacity of this organism. Structures of four enzymes were determined and analyzed to assess their potential in improving the bioremediation process: THBD RW1, an enzyme that is relatively more resistant to inactivation; DoxG-SMA2, a directed evolution mutant more active than DHBDLB400 and its wild-type against certain metabolites; DHBDP6-I and -III, two enzymes with complementary substrate specificities, which have higher specificity than DHBDLB400 for certain monochlorinated metabolites. Their structural analysis presented new opportunities for improvement of the bioremediation process by recruiting and improving these enzymes through selected or directed modifications.

ISBN: 9780549357551Subjects--Topical Terms:

1019105
Biophysics, General.

Structural studies on extradiol dioxygenases: Strategies for improved bioremediation of PCBs.
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020 $a 9780549357551
035 $a (UMI)AAI3291071
035 $a AAI3291071
040 $a UMI $c UMI
100 1 $a Koksal, Mustafa. $3 1285871
245 1 0 $a Structural studies on extradiol dioxygenases: Strategies for improved bioremediation of PCBs.
300 $a 240 p.
500 $a Adviser: Jeffrey T. Bolin.
500 $a Source: Dissertation Abstracts International, Volume: 68-12, Section: B, page: 7865.
502 $a Thesis (Ph.D.)--Purdue University, 2007.
520 $a Bioremediation has emerged as a possible alternative to other non-biological methods to eliminate polychlorinated biphenyls (PCBs). However, there are limitations due to inabilities of the microorganisms that may be used in this process. 2,3-dihydroxybiphenyl-1,2-dioxygenase (DHBD), which cleaves the aromatic ring of PCBs, is one of the key enzymes in the biodegradation pathway, determining the ability of an organism to degrade a wide variety of PCBs. Burkholderia xenovorans strain LB400 is a potential candidate organism for bioremediation applications, however, DHBDLB400 suffers from substrate-facilitated suicide inactivation, poor catalytic activity and low substrate specificity for some PCB congeners. Supplementation of the organism with DHBD variants from other pathways was considered as a powerful strategy to improve the capacity of this organism. Structures of four enzymes were determined and analyzed to assess their potential in improving the bioremediation process: THBD RW1, an enzyme that is relatively more resistant to inactivation; DoxG-SMA2, a directed evolution mutant more active than DHBDLB400 and its wild-type against certain metabolites; DHBDP6-I and -III, two enzymes with complementary substrate specificities, which have higher specificity than DHBDLB400 for certain monochlorinated metabolites. Their structural analysis presented new opportunities for improvement of the bioremediation process by recruiting and improving these enzymes through selected or directed modifications.
590 $a School code: 0183.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0487
690 $a 0786
710 2 $a Purdue University. $b Biological Sciences. $3 1285872
773 0 $t Dissertation Abstracts International $g 68-12B.
790 $a 0183
790 1 0 $a Bolin, Jeffrey T., $e advisor
790 1 0 $a Rossmann, Michael G. $e committee member
790 1 0 $a Stauffacher, Cynthia V. $e committee member
790 1 0 $a van Etten, Robert L. $e committee member
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3291071