Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin

被引:123
|
作者
Parsonage, Derek [1 ]
Karplus, P. Andrew [2 ]
Poole, Leslie B. [1 ]
机构
[1] Wake Forest Univ, Bowman Gray Sch Med, Dept Biochem, Winston Salem, NC 27157 USA
[2] Oregon State Univ, Dept Biochem & Biophys, Corvallis, OR 97331 USA
关键词
antioxidants; peroxidases; redox regulation; redox-active disulfide;
D O I
10.1073/pnas.0708308105
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
Typical 2-Cys peroxiredoxins (Prxs) are ubiquitous peroxidases that are involved in peroxide scavenging and/or the regulation of peroxide signaling in eukaryotes. Despite their prevalence, very few Prxs have been reliably characterized in terms of their substrate specificity profile and redox potential even though these values are important for gaining insight into physiological function. Here, we present such studies focusing on Salmonella typhimurium alkyl hydroperoxide reductase C component (StAhpC), an enzyme that has proven to be an excellent prototype of this largest and most widespread class of Prxs that includes mammalian Prx I-Prx IV. The catalytic efficiencies of StAhpC (k(cat)/K-m) are > 10(7) M-1.s(-1) for inorganic and primary hydroperoxide substrates and approximate to 100-fold less for tertiary hydroperoxides, with the difference being exclusively caused by changes in K-m. The oxidative inactivation of AhpC through reaction with a second molecule of peroxide shows parallel substrate specificity. The midpoint reduction potential of StAhpC is determined to be -178 +/- 0.4 mV, a value much higher than most other thiol-based redox proteins. The relevance of these results for our understanding of Prx and the physiological role of StAhpC is discussed.
引用
收藏
页码:8209 / 8214
页数:6
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