Summary
Crystal structure of bovine heart cytochrome c oxidase at fully oxidized state at 2.8 Å resolution shows that this protein consists of 13 different subunits, each in one copy, and 8 phospholipids in addition to 7 metal ions, 2 irons, 3 coppers, 1 magnesium, and 1 zinc. Three redox active sites, CuA, heme a, and the O2 reduction site containing heme a 3 and CuB, are connected by three possible pathways for facile electron transfers. The pathways between CuA and heme a and between heme a and heme a 3 are consistent with the rapid electron transfers determined kinetically. However, the role of the direct pathway between CuA and heme a 3 is unknown. The coordination geometry of CuB together with the proximity between the two hemes suggest that heme a, not CuB, donates electrons to initiate the reduction of O2 in the two electron process. Tyr244 is identified as the proton donor for producing water from the intermediates during O2 reduction. Possible proton-pumping sites are mapped well separated from the O2 reduction site. No possible proton-pumping site involving the O2 reduction site has been identified, suggesting an indirect coupling between O2 reduction and proton pumping.
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Yoshikawa, S., Shinzawa-Itoh, K., Tsukihara, T. (1998). Crystal Structure and Reaction Mechanism of Bovine Heart Cytochrome c Oxidase. In: Ishimura, Y., Shimada, H., Suematsu, M. (eds) Oxygen Homeostasis and Its Dynamics. Keio University Symposia for Life Science and Medicine, vol 1. Springer, Tokyo. https://doi.org/10.1007/978-4-431-68476-3_2
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DOI: https://doi.org/10.1007/978-4-431-68476-3_2
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