Heme binding and polymerization by Plasmodium falciparum histidine rich protein II: influence of pH on activity and conformation

Lynn, Andrew ; Chandra, Shweta ; Malhotra, Pawan ; Chauhan, Virander S. (1999) Heme binding and polymerization by Plasmodium falciparum histidine rich protein II: influence of pH on activity and conformation FEBS Letters, 459 (2). pp. 267-271. ISSN 0014-5793

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Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related URL: http://dx.doi.org/10.1016/S0014-5793(99)01260-0

Abstract

The histidine rich protein II (HRPII) from Plasmodium falciparum has been implicated as a heme polymerase which detoxifies free heme by its polymerization to inactive hemozoin. Histidine-iron center coordination is the dominant mechanism of interaction between the amino acid and heme. The protein also contains aspartate allowing for ionic/coordination interactions between the carboxylate side chain and the heme metal center. The pH profile of heme binding and polymerization shows the possibility of these two types of binding sites being differentiated by pH. Circular dichroism studies of the protein show that pH and heme binding cause a change in conformation above pH 6 implying the involvement of His-His+ transitions. Heme binding at pHs above 6 perturbs HRPII conformation, causing an increase in helicity.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
ID Code:77465
Deposited On:12 Jan 2012 14:42
Last Modified:12 Jan 2012 14:42

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