Unknown

Dataset Information

0

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

ABSTRACT: 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.

SUBMITTER: Lei C 

PROVIDER: S-EPMC3005779 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

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

Lei Cheng C   Rider S Dean SD   Wang Cai C   Zhang Haili H   Tan Xiangshi X   Zhu Guan G  

Protein science : a publication of the Protein Society 20101101 11

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  ...[more]

Similar Datasets

Unknown NADP(H) allosterically regulates the interaction between ferredoxin and ferredoxin-NADP+ reductase.
| S-EPMC6886308 | biostudies-literature
Unknown Ferredoxin-NADP+ reductase from Pseudomonas putida functions as a ferric reductase.
| S-EPMC2648195 | biostudies-literature
Transcriptomics Lifecycle progression and sexual development of the apicomplexan parasite Cryptosporidium parvum
2019-09-03 | GSE129267 | GEO
Unknown Docking analysis of transient complexes: interaction of ferredoxin-NADP+ reductase with ferredoxin and flavodoxin.
| S-EPMC4162409 | biostudies-literature
Unknown Unique Tubulin-Based Structures in the Zoonotic Apicomplexan Parasite Cryptosporidium parvum.
| S-EPMC8464796 | biostudies-literature
Unknown Protein coding gene nucleotide substitution pattern in the apicomplexan protozoa Cryptosporidium parvum and Cryptosporidium hominis.
| S-EPMC2413048 | biostudies-literature
Unknown Crystal structures of Leptospira interrogans FAD-containing ferredoxin-NADP+ reductase and its complex with NADP+.
| S-EPMC2148051 | biostudies-literature
Unknown Life cycle progression and sexual development of the apicomplexan parasite Cryptosporidium parvum.
| S-EPMC6877471 | biostudies-literature
Unknown Biosynthesis of Orthogonal Molecules Using Ferredoxin and Ferredoxin-NADP+ Reductase Systems Enables Genetically Encoded PhyB Optogenetics.
| S-EPMC5820651 | biostudies-literature
Unknown Functional characterization of an evolutionarily distinct phosphopantetheinyl transferase in the apicomplexan Cryptosporidium parvum.
| S-EPMC1168963 | biostudies-literature