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August 24, 2026Journal of Molecular BiologyOpen Access

A Divergent Mitochondrial Cytochrome c in Malaria Parasites With an Anomalously Low Redox Potential

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Authors

KLKade M. LoveridgeOOOtessa D OlsenSSSamuel R. Scherer

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Overview

Biochemical analysis uncovers an anomalously low redox potential in Plasmodium falciparum cytochrome c-2, suggesting non-canonical biological roles beyond the classic electron transport chain.

Key Points

  • To identify and characterize the biochemical, structural, and redox properties of a newly recognized mitochondrial cytochrome c lineage in Apicomplexan malaria parasites.
  • Identified a divergent eukaryotic cytochrome c homolog (Pfcyt c-2) from Plasmodium falciparum.
  • Assessed heme coordination, redox potential, enzymatic peroxidase activity, and thermal stability of the purified protein.
  • Pfcyt c-2 demonstrated an anomalously low redox potential of -278 ± 6 mV, more than 500 mV lower than canonical mitochondrial cytochrome c (+250 mV).
  • Heterogeneous heme coordination was observed despite the structural conservation of canonical His/Met axial ligands.
  • The protein maintained low-level peroxidase activity and global thermostability comparable to canonical cytochrome c proteins.

Cite This Study

Loveridge et al. (2026) studied this question.

synapsesocial.com/papers/6aa92108d6d58a1cc10c0207https://doi.org/10.1016/j.jmb.2026.169996
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