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Heme is a small, iron-containing, planar molecule (iron protoporphyrin IX) that acts as a prototypical prosthetic group in a broad range of proteins—most notably hemoglobin, myoglobin, cytochromes, catalases, and peroxidases. It is essential for oxygen transport, electron transfer, catalysis, and as a sensor and regulator of cellular redox status[1][2][4][7]. In infectious diseases such as malaria, the parasite degrades hemoglobin and releases free heme, which is toxic; the parasite detoxifies it by biocrystallization (hemozoin formation), a process exploited by numerous antimalarial drugs. Various parasite proteins is not a valid target name; it is overly broad and does not correspond to a defined molecular entity or drug target class but instead refers to the numerous proteins found in parasites. To be meaningful for scientific or therapeutic targeting, individual proteins should be identified (e.g., "Plasmodium falciparum dihydrofolate reductase").
Antimalarials (e.g., artemisinin, chloroquine) interact with heme by either producing toxic radicals in the presence of heme or by inhibiting heme detoxification pathways in the parasite, leading to parasite death[1].
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