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Application of EPR spectroscopy to s...

Girotto, Stefania.

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Application of EPR spectroscopy to study the resting state structure and the mechanism of Mycobacterium tuberculosis catalase-peroxidase (KatG).

Record Type:	Electronic resources : Monograph/item
Title/Author:	Application of EPR spectroscopy to study the resting state structure and the mechanism of Mycobacterium tuberculosis catalase-peroxidase (KatG)./
Author:	Girotto, Stefania.
Description:	157 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-12, Section: B, page: 6101.
Contained By:	Dissertation Abstracts International64-12B.
Subject:	Chemistry, Physical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3115252

Application of EPR spectroscopy to study the resting state structure and the mechanism of Mycobacterium tuberculosis catalase-peroxidase (KatG).
Girotto, Stefania.

Application of EPR spectroscopy to study the resting state structure and the mechanism of Mycobacterium tuberculosis catalase-peroxidase (KatG). - 157 p.

Source: Dissertation Abstracts International, Volume: 64-12, Section: B, page: 6101.

Thesis (Ph.D.)--City University of New York, 2004.

Mycobacterium tuberculosis (M. tuberculosis ) catalase-peroxidase (KatG) is a dimeric Class I heme peroxidase whose activity is implicated for the activation of the anti-tuberculosis antibiotic isoniazid (INH).Subjects--Topical Terms:

560527
Chemistry, Physical.

Application of EPR spectroscopy to study the resting state structure and the mechanism of Mycobacterium tuberculosis catalase-peroxidase (KatG).
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035 $a (UnM)AAI3115252
035 $a AAI3115252
040 $a UnM $c UnM
100 1 $a Girotto, Stefania. $3 1950168
245 1 0 $a Application of EPR spectroscopy to study the resting state structure and the mechanism of Mycobacterium tuberculosis catalase-peroxidase (KatG).
300 $a 157 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-12, Section: B, page: 6101.
500 $a Adviser: Richard S. Magliozzo.
502 $a Thesis (Ph.D.)--City University of New York, 2004.
520 $a Mycobacterium tuberculosis (M. tuberculosis ) catalase-peroxidase (KatG) is a dimeric Class I heme peroxidase whose activity is implicated for the activation of the anti-tuberculosis antibiotic isoniazid (INH).
520 $a The catalytic function and the structure of this enzyme have been examined using rapid freeze-quench (RFQ and low temperature X-band EPR spectroscopy.
520 $a The enzyme exhibits catalytic properties that differ from the Class I peroxidases. The reaction of ferric KatG with peroxyacetic acid was followed using RFQ-EPR (77 K). A doublet EPR signal appears within 6.4 ms after mixing and at time points t
520 $a Single amino acid replacements in KatG have been investigated as a direct approach to identify the tyrosine residues at which the radical(s) is formed. RFQ-EPR spectroscopy confirms that tyrosine Y353, unique to M. tuberculosis KatG, is the ami
520 $a Low temperature EPR studies of ferric KatG, supported by optical and Raman data, suggest that different factors, such as water and other ligand binding, protonation state of the distal imidazole and incomplete adduct formation, are responsible f
590 $a School code: 0046.
650 4 $a Chemistry, Physical. $3 560527
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
690 $a 0494
690 $a 0487
690 $a 0786
710 2 0 $a City University of New York. $3 1018111
773 0 $t Dissertation Abstracts International $g 64-12B.
790 1 0 $a Magliozzo, Richard S., $e advisor
790 $a 0046
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3115252