On 2013 Jun 16, Akhil Vaidya commented:

Malaria parasites generate millimolar concentration of heme inside the infected RBC as a consequence of hemoglobin digestion. It is generally accepted that all this heme is detoxified within the parasite food vacuole to produce hematin crystals. On the other habd, if this heme was available as a substrate for heme oxygenase, one can imagine significant generation of biliverdine and carbon monoxide in infected RBC. Therefore, identification of a gene encoding a protein with significant homology to heme oxygenase was a surprise. The paper by Sigala et al., however, lays to rest this possibility by conclusively showing that infected RBC contain no more biliverdine or bilirubin than uninfected RBC, and that the annotated heme oxygenase of Plasmodium falciparum has little enzymatic activity expected. Thus, this protein, which is conserved among all species of malaria parasites, is likely to have acquired a new function while losing its enzymatic activity. It would be of interest to find out what this function could be.

On 2013 Jun 16, Akhil Vaidya commented:

Malaria parasites generate millimolar concentration of heme inside the infected RBC as a consequence of hemoglobin digestion. It is generally accepted that all this heme is detoxified within the parasite food vacuole to produce hematin crystals. On the other habd, if this heme was available as a substrate for heme oxygenase, one can imagine significant generation of biliverdine and carbon monoxide in infected RBC. Therefore, identification of a gene encoding a protein with significant homology to heme oxygenase was a surprise. The paper by Sigala et al., however, lays to rest this possibility by conclusively showing that infected RBC contain no more biliverdine or bilirubin than uninfected RBC, and that the annotated heme oxygenase of Plasmodium falciparum has little enzymatic activity expected. Thus, this protein, which is conserved among all species of malaria parasites, is likely to have acquired a new function while losing its enzymatic activity. It would be of interest to find out what this function could be.