The apicomplexan Cryptosporidium parvum possesses a single mitochondrial-type ferredoxin and ferredoxin:NADP+ reductase system

被引:4
作者
Lei, Cheng [1 ,2 ]
Rider, S. Dean, Jr. [3 ]
Wang, Cai [1 ,2 ]
Zhang, Haili [3 ]
Tan, Xiangshi [1 ,2 ,3 ]
Zhu, Guan [3 ,4 ]
机构
[1] Fudan Univ, Dept Chem, Shanghai 200433, Peoples R China
[2] Fudan Univ, Inst Biomed Sci, Shanghai 200433, Peoples R China
[3] Texas A&M Univ, Coll Vet Med & Biomed Sci, Dept Vet Pathobiol, College Stn, TX 77840 USA
[4] Texas A&M Univ, Fac Genet Program, College Stn, TX 77840 USA
基金
中国国家自然科学基金; 美国国家卫生研究院;
关键词
apicomplexan; Cryptosporidium; ferredoxin; ferredoxin:NADP(+) reductase; electron transfer; HUMAN MALARIA PARASITE; FATTY-ACID SYNTHESIS; TOXOPLASMA-GONDII; ESCHERICHIA-COLI; IN-VITRO; PLASMODIUM-FALCIPARUM; EIMERIA-TENELLA; GENOME-SEQUENCE; APICOPLAST; OXIDOREDUCTASE;
D O I
10.1002/pro.487
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We have successfully expressed recombinant mitochondrial-type ferredoxin (mtFd) and ferredoxin:NADP(+) reductase (mtFNR) from Ctyptosporidium parvum and characterized their biochemical features for the first time for an apicomplexan. Both C. parvum mtFd (CpmtFd) and FNR (CpmtFNR) were obtained and purified as holo-proteins, in which the correct assembly of [2Fe-2S] cluster in Fd and that of FAD in FNR were confirmed and characterized by UV/vis and electron paramagnetic resonance. These proteins were fully functional and CpmtFNR was capable of transferring electrons from NADPH to CpmtFd in a cytochrome c-coupled assay that followed a typical Michaelis-Menten kinetics. Apicomplexan mtFd and mtFNR proteins were evolutionarily divergent from their counterparts in humans and animals and could be explored as potential drug targets in Cryptosporidium and other apicomplexans.
引用
收藏
页码:2073 / 2084
页数:12
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