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Both <jats:italic>C. parvum<\/jats:italic> mtFd (CpmtFd) and FNR (CpmtFNR) were obtained and purified as holo\u2010proteins, in which the correct assembly of [2Fe\u20132S] 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 <jats:italic>c<\/jats:italic>\u2010coupled assay that followed a typical Michaelis\u2010Menten 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 <jats:italic>Cryptosporidium<\/jats:italic> and other apicomplexans.<\/jats:p>","DOI":"10.1002\/pro.487","type":"journal-article","created":{"date-parts":[[2010,8,29]],"date-time":"2010-08-29T18:29:12Z","timestamp":1283106552000},"page":"2073-2084","source":"Crossref","is-referenced-by-count":7,"title":["The apicomplexan <i>Cryptosporidium parvum<\/i> possesses a single mitochondrial\u2010type ferredoxin and ferredoxin:NADP<sup>+<\/sup> reductase system"],"prefix":"10.1002","volume":"19","author":[{"given":"Cheng","family":"Lei","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"suffix":"Jr.","given":"S. 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