ArticleJournal of molecular biology2026
A Divergent Mitochondrial Cytochrome c in Malaria Parasites With an Anomalously Low Redox Potential.
Article in Journal of molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Eukaryotic cytochrome (cyt) c is a highly conserved mitochondrial protein central to cellular respiration, featuring a covalently attached heme with hexacoordinate iron whose redox potential is tuned by axial His/Met ligands and surrounding residues to support electron transport chain (ETC) function. We have identified a previously unrecognized lineage of eukaryotic cyt c homologs in Apicomplexa, a phylum of intracellular pathogens that includes Plasmodium falciparum malaria parasites. P. falciparum cyt c-2 (Pfcyt c-2) exemplifies this divergent lineage and displays heterogeneous heme coordination despite conservation of His/Met ligands. We determined that Pfcyt c-2 has a redox potential of -278 ± 6 mV that is over 500 mV lower than canonical mitochondrial cyt c homologs (+250 mV) and contradicts a conserved ETC role. This anomalous redox potential is lower than any natural monoheme c-type cyt and reveals exceptional evolutionary tuning for a eukaryotic cyt c. Although Pfcyt c-2 displays signs of structural heterogeneity, it retains low-level peroxidase activity and global protein thermostability comparable to canonical cyt c proteins. These results reveal a new clade of eukaryotic cyt c proteins with divergent biochemical properties and biological roles, opening new scaffolds for mechanistic discovery and redox engineering of natural and abiological functions.
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