Cytochrome c oxidase subunit III is one of main transmembrane subunits of cytochrome c oxidase

Cytochrome c oxidase () is the terminal enzyme of the respiratory chain of mitochondria and many aerobic bacteria. It catalyzes the transfer of electrons from reduced cytochrome c to molecular oxygen:

4 cytochrome c⁺² + 4 H⁺ + O₂ \rightleftharpoons 4 cytochrome c⁺³ + 2 H₂O

This reaction is coupled to the pumping of four additional protons across the mitochondrial or bacterial membrane^[1][2].

Cytochrome c oxidase is an oligomeric enzymatic complex that is located in the mitochondrial inner membrane of eukaryotes and in the plasma membrane of aerobic prokaryotes. The core structure of prokaryotic and eukaryotic cytochrome c oxidase contains three common subunits, I, II and III. In prokaryotes, subunits I and III can be fused and a fourth subunit is sometimes found, whereas in eukaryotes there are a variable number of additional small subunits^[3].

As the bacterial respiratory systems are branched, they have a number of distinct terminal oxidases, rather than the single cytochrome c oxidase present in the eukaryotic mitochondrial systems. Although the cytochrome o oxidases do not catalyze the cytochrome c but the quinol (ubiquinol) oxidation they belong to the same haem-copper oxidase superfamily as cytochrome c oxidases. Members of this family share sequence similarities in all three core subunits: subunit I is the most conserved subunit, whereas subunit II is the least conserved^[4][5][6].

Subfamilies

• Cytochrome o ubiquinol oxidase, subunit III
• Cytochrome aa3 quinol oxidase, subunit III

Human proteins containing this domain

CO3; COIII; COX3; MT-CO3;

References

Further reading

The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A. Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S; Science 1996;272:1136-1144.

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