Protein science : a publication of the Protein Society · 2010
The apicomplexan Cryptosporidium parvum possesses a single mitochondrial-type ferredoxin and ferredoxin:NADP+ reductase system.
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Lei Cheng, Rider S Dean, Wang Cai, Zhang Haili, Tan Xiangshi, Zhu Guan
Аннотация
We have successfully expressed recombinant mitochondrial-type ferredoxin (mtFd) and ferredoxin:NADP(+) reductase (mtFNR) from Cryptosporidium 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.
Предметные рубрики MeSH
Amino Acid SequenceAnimalsCloning, MolecularCryptosporidium parvumElectron TransportElectrophoresis, Polyacrylamide GelFerredoxin-NADP ReductaseFerredoxinsGene Expression ProfilingHumansLife Cycle StagesMitochondrial ProteinsMolecular Sequence AnnotationMolecular Sequence DataPhylogenyProtozoan ProteinsReverse Transcriptase Polymerase Chain ReactionSequence AlignmentSpectrophotometry, Ultraviolet