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- W2117260327 abstract "The transient interactions of respiratory cytochrome c with complexes III and IV is herein investigated by using heterologous proteins, namely human cytochrome c, the soluble domain of plant cytochrome c1 and bovine cytochrome c oxidase. The binding molecular mechanisms of the resulting cross-complexes have been analyzed by Nuclear Magnetic Resonance and Isothermal Titration Calorimetry. Our data reveal that the two cytochrome c-involving adducts possess a 2:1 stoichiometry - that is, two cytochrome c molecules per adduct - at low ionic strength. We conclude that such extra binding sites at the surfaces of complexes III and IV can facilitate the turnover and sliding of cytochrome c molecules and, therefore, the electron transfer within respiratory supercomplexes." @default.
- W2117260327 created "2016-06-24" @default.
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- W2117260327 date "2015-01-13" @default.
- W2117260327 modified "2023-10-18" @default.
- W2117260327 title "Respiratory complexes III and IV can each bind two molecules of cytochrome<i>c</i>at low ionic strength" @default.
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- W2117260327 doi "https://doi.org/10.1016/j.febslet.2015.01.004" @default.
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