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Title: Hydrogen Peroxide-Mediated Isoniazid Activation Catalyzed by Mycobacterium tuberculosis Catalase-Peroxidase (KatG) and Its S315T Mutant

Authors:
; ; ; ; ;  [1];  [2]
  1. (Brooklyn C.)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
DOE - BASIC ENERGY SCIENCES
OSTI Identifier:
1170423
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemistry-US; Journal Volume: 45; Journal Issue: (13) ; 03, 2006
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Zhao, Xiangbo, Yu, Hong, Yu, Shengwei, Wang, Feng, Sacchettini, James C., Magliozzo, Richard S., and TAM). Hydrogen Peroxide-Mediated Isoniazid Activation Catalyzed by Mycobacterium tuberculosis Catalase-Peroxidase (KatG) and Its S315T Mutant. United States: N. p., 2015. Web. doi:10.1021/bi051967o.
Zhao, Xiangbo, Yu, Hong, Yu, Shengwei, Wang, Feng, Sacchettini, James C., Magliozzo, Richard S., & TAM). Hydrogen Peroxide-Mediated Isoniazid Activation Catalyzed by Mycobacterium tuberculosis Catalase-Peroxidase (KatG) and Its S315T Mutant. United States. doi:10.1021/bi051967o.
Zhao, Xiangbo, Yu, Hong, Yu, Shengwei, Wang, Feng, Sacchettini, James C., Magliozzo, Richard S., and TAM). Thu . "Hydrogen Peroxide-Mediated Isoniazid Activation Catalyzed by Mycobacterium tuberculosis Catalase-Peroxidase (KatG) and Its S315T Mutant". United States. doi:10.1021/bi051967o.
@article{osti_1170423,
title = {Hydrogen Peroxide-Mediated Isoniazid Activation Catalyzed by Mycobacterium tuberculosis Catalase-Peroxidase (KatG) and Its S315T Mutant},
author = {Zhao, Xiangbo and Yu, Hong and Yu, Shengwei and Wang, Feng and Sacchettini, James C. and Magliozzo, Richard S. and TAM)},
abstractNote = {},
doi = {10.1021/bi051967o},
journal = {Biochemistry-US},
number = (13) ; 03, 2006,
volume = 45,
place = {United States},
year = {Thu Feb 12 00:00:00 EST 2015},
month = {Thu Feb 12 00:00:00 EST 2015}
}
  • Genetic deficiencies of glucose-6-phosphate dehydrogenase (G6PD) and NADPH predispose affected erythrocytes to destruction from peroxides. Conversely, genetic deficiencies of catalase do not predispose affected erythrocytes to peroxide-induced destruction. These observations have served to strengthen the assumption that the NADPH/glutathione/glutathione peroxidase pathway is the principal means for disposal of H/sub 2/O/sub 2/ in human erythrocytes. Recently, however, mammalian catalase was found to have tightly bound NADPH and to require NADPH for the prevention and reversal of inactivation by its toxic substrate (H/sub 2/O/sub 2/). Since both catalase and the glutathione pathway are dependent on NADPH for function, this finding raises themore » possibility that both mechanisms destroy H/sub 2/O/sub 2/ in human erythrocytes. A comparison of normal and acatalasemic erythrocytes in the present study indicated that catalase accounts for more than half of the destruction of H/sub 2/O/sub 2/ when H/sub 2/O/sub 2/ is generated at a rate comparable to that which leads to hemolysis in G6PD- deficient erythrocytes.« less
  • Data are reviewed on the relationship between hydrogen peroxide and x radiation effects in formed cancer cells. Topics discussed include the interrelationships between hydrogen peroxide, catalase, glutathione, peroxidase, quinones, nordihydroguaiaretic acid, and phosphopyridine nucleotides in relation to metabolism in irradiated cancer cells. The metabolic sites of action of chemotherapeutic agents and metabolic and biochemical mechanisms involved in the action of x radiation are considered. (C.H.)
  • Data are presented te show that high levels of catalase in Rhodopseudomonas spberoides protect sgainst inactivation by added hydrogen peroxide but not against inactivation by x irradiation. The degree of protection against hydrogen peroxide is in good agreement with theoretical predictions. Oxygen enlances damsge by x irradiation but reduces damage caused by hydrogen peroxide diffusion into the cell. lt is concluded that diffusing hydrogen peroxide is not a major intermediate in radiation damage of these cells. (auth)
  • The effect of hydrogen peroxide and phenolic compounds on the decolorization of betanin and a betaxanthin preparation by horse-radish peroxidase (HRP) was examined. Betanin was decolorized at a greater rate than the betaxanthin pigments and both reactions were H/sub 2/O/sub 2/-dependent. Betaxanthin was more prone to oxidatic decolorization than betanin. 2,4-Dichlorophenol, resorcinol and o-toluidine stimulated the decolorization of both pigments. Guaiacol enhanced the peroxidatic decolorization of both pigments to a small extent, but inhibited the oxidatic breakdown of betaxanthin. Possible implications of these results are discussed. 17 references, 4 figures.