Catalases Are NAD(P)H-Dependent Tellurite Reductases

被引:70
作者
Calderon, Ivan L. [1 ]
Arenas, Felipe A. [1 ]
Perez, Jose Manuel [1 ]
Fuentes, Derie E. [1 ]
Araya, Manuel A. [1 ]
Saavedra, Claudia P. [2 ]
Tantalean, Juan C. [3 ]
Pichuantes, Sergio E. [4 ]
Youderian, Philip A. [5 ]
Vasquez, Claudio C. [1 ]
机构
[1] Univ Santiago Chile, Fac Quim & Biol, Mol Microbiol Lab, Santiago, Chile
[2] Univ Andres Bello, Fac Ciencias Salud, Lab Microbiol Mol & Biotecnol, Santiago, Chile
[3] Univ San Luis Gonzaga Ica, Fac Ciencias, Lab Microbiol Ind & Biotecnol, Ica, Peru
[4] Chiron Corp, Blood Testing Div, Emeryville, CA 94608 USA
[5] Texas A&M Univ, Dept Biol, College Stn, TX 77843 USA
来源
PLOS ONE | 2006年 / 1卷 / 01期
基金
美国国家卫生研究院;
关键词
D O I
10.1371/journal.pone.0000070
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Reactive oxygen species damage intracellular targets and are implicated in cancer, genetic disease, mutagenesis, and aging. Catalases are among the key enzymatic defenses against one of the most physiologically abundant reactive oxygen species, hydrogen peroxide. The well-studied, heme-dependent catalases accelerate the rate of the dismutation of peroxide to molecular oxygen and water with near kinetic perfection. Many catalases also bind the cofactors NADPH and NADH tenaciously, but, surprisingly, NAD(P)H is not required for their dismutase activity. Although NAD(P)H protects bovine catalase against oxidative damage by its peroxide substrate, the catalytic role of the nicotinamide cofactor in the function of this enzyme has remained a biochemical mystery to date. Anions formed by heavy metal oxides are among the most highly reactive, natural oxidizing agents. Here, we show that a natural isolate of Staphylococcus epidermidis resistant to tellurite detoxifies this anion thanks to a novel activity of its catalase, and that a subset of both bacterial and mammalian catalases carry out the NAD(P)H-dependent reduction of soluble tellurite ion (TeO32-) to the less toxic, insoluble metal, tellurium (Te degrees), in vitro. An Escherichia coli mutant defective in the KatG catalase/peroxidase is sensitive to tellurite, and expression of the S. epidermidis catalase gene in a heterologous E. coli host confers increased resistance to tellurite as well as to hydrogen peroxide in vivo, arguing that S. epidermidis catalase provides a physiological line of defense against both of these strong oxidizing agents. Kinetic studies reveal that bovine catalase reduces tellurite with a low Michaelis-Menten constant, a result suggesting that tellurite is among the natural substrates of this enzyme. The reduction of tellurite by bovine catalase occurs at the expense of producing the highly reactive superoxide radical.
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页数:8
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