The proteins found in the mitochondria of apicomplexan parasites, including key proteins involved in energy generation, are very different from mitochondrial proteins of the animals these parasites infect.

Biochemical analyses show that mitochondrial COX16 assists in the process of copper insertion into COX2 and reveal a second COX16 function in linking assembly routes of the redox center-containing COX1 and COX2 subunits.

The cancer testis antigen COX6B2 enhances cytochrome c oxidase activity thereby promoting proliferation and survival in cancer cells and represents a therapeutic target for inhibiting oxidative phosphorylation selectively in tumors.

Beneficial symbiotic bacteria encode an exceptional number of toxin-related genes that are all expressed by the symbionts in the host, supporting their key role in host-microbe interactions.

During growth in biofilms and host infection, the opportunistic pathogen Pseudomonas aeruginosa employs respiratory heterocomplexes that support extracellular electron shuttling and pathogenicity.

Promoting a Warburg-like shift in astrocytic metabolism through reduced mitochondrial electron transport accommodates the energetic burden caused by brain trauma without overwhelming cellular respiration and redox to salvage dopaminergic neurons.

Interactions among parasites in snails create cascading effects on their transmission and highlight that biodiversity has complex, context-dependent and important effects on human schistosomiasis transmission dynamics.

Cryo-EM structure of the mammalian respiratory supercomplex containing complexes I, III and IV shows a functional asymmetry of complex III, providing strong evidence for directed electron flow in the respirasome.

Building on previous work (Guarani et al., 2015), MICOS (mitochondrial contact site) assembly and cristae junction formation are shown to have a critical role in human health.

The use of genetically encoded redox sensors in phagocytized bacteria reveals that, among the toxic cocktail of oxidants released into the neutrophil's phagolysosome, HOCl is the main component responsible for the oxidative modification of bacterial protein thiols.