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Spectroscopic studies showed that a single HRP II molecule may bind to multiple heme molecules [ 59].
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In chemical terms, RBC turnover would release substantial amounts of heme (∼6×108 heme molecules per RBC).
It was further demonstrated that purified crystal consists only of heme molecules [15] being chemically and structurally identical to a synthetic heme crystal known as βH [16].
Therefore, a proposed model suggested that, to produce βH crystals, heme dimers are formed by means of reciprocal iron-carboxylate linkage between heme molecules, which would require the displacement of the axial water molecule bound to the porphyrin [24], [27].
HRP-II might facilitate Hz formation by binding with a large number of heme molecules, and facilitating dimer formation involving iron-carboxylate bonds between every two heme molecules [17].
Molecular dynamics simulations demonstrated that H2O ferriprotoporphyrin IX molecules interact quite fast, producing the βH precursor by means of reciprocal iron-propionate attraction between heme molecules [24].
Hemozoin strongly absorbs UV light resulting in vaporization of individual heme molecules.
We therefore evaluated the protein-induced conformational changes of the heme molecules using CD.
First, several parasite genes that encode the enzymes used to make heme molecules were deleted.
Cytochromes b561 are intrinsic membrane proteins containing two heme molecules, and reducible by ascorbate.
Hence the estimated binding sites of heme molecules are around 15 18.
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