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By Gould R.F. (ed.)

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Structure of redox active metal cofactors in CcO (figure prepared in PyMOL). Electrons are deliveredfrom cytochrome c to the dinuclear Cu site (upper) before being transferred to heme A (lower left). The electrons are then shuttled to the heterobimetallic hemeA-Cu site (lower right) where O2 is reduced to water. The original coordinates are available in reference 14. A B electron acceptor and therefore aids in CcO activity, while the farnesyl moiety serves to anchor heme A in the enzyme and prevent the heme from dissociating when oxidized to the ferric state.

Coxl, the largest and most hydrophobic subunit, is composed of 12 transmembrane helices and contains two redox active metal centers, heme a and a heme a -Cue binuclear metal center. Coxl also contains one sodium ion, although the functional significance of this site is not currently known. Cox2, the smallest and the least hydrophobic core subunit with only two transmembrane helices, contains the binuclear mixed-valent C u site. The function of the magnesium ion found at the interface of Coxl and Cox2 remains unknown, although it may help to prevent the back-leak of protons through the water-exit channel (12).

Human frataxin has an additional 17 amino acid Cterminal tail that is essential for protein stability (25) and which structurally folds against frataxin's helical ferrochelatase binding plane (26). In addition, human frataxin/ferrochelatase studies were performed on an N-terminally truncated form of frataxin that may modulate binding between the protein partners (10). Finally, human ferrochelatase has an Fe-S cluster that is not present in the yeast ortholog, and this divergence might account for altered protein interactions (27).

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Applied Chemistry at Protein Interfaces by Gould R.F. (ed.)

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