title: Heme-binding properties of heme detoxification protein from Plasmodium falciparum.
abstract: The heme detoxification protein of the malaria parasite Plasmodium falciparum is involved in the formation of hemozoin, an insoluble crystalline form of heme. Although the disruption of hemozoin formation is the most widely used strategy for controlling the malaria parasite, the heme-binding properties of heme detoxification protein are poorly characterized. In this study, we established a method for the expression and purification of the non-tagged protein and characterized heme-binding properties. The spectroscopic features of non-tagged protein differ from those of the His-tagged protein, suggesting that the artificial tag interferes with the properties of the recombinant protein. The purified recombinant non-tagged heme detoxification protein had two heme-binding sites and exhibited a spectrum typical of heme proteins. A mechanism for hemozoin formation is proposed.
authors.affiliation: Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
authors.forename: Keisuke
authors.initials: K
authors.lastname: Nakatani
authors.forename: Haruto
authors.initials: H
authors.lastname: Ishikawa
authors.forename: Shigetoshi
authors.initials: S
authors.lastname: Aono
authors.forename: Yasuhisa
authors.initials: Y
authors.lastname: Mizutani
mesh_terms: D001665:Binding Sites; D006418:Heme / Q000737:chemistry* / Q000378:metabolism; D010963:Plasmodium falciparum / Q000378:metabolism*; D015800:Protozoan Proteins / Q000737:chemistry* / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: C529576:HDP protein, Plasmodium falciparum; D015800:Protozoan Proteins; D011994:Recombinant Proteins; D006418:Heme
keywords: Crystallization; Heme; Malaria; Spectroscopy