PROSITE documentation PDOC50253Heme-copper oxidase subunit III profile
Cytochrome c oxidase (EC 1.9.3.1) 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. This reaction is coupled to the pumping of four additional protons across the mitochondrial or bacterial membrane [1].
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 polypeptidic subunits [2]. The functional role of subunit III is not yet understood.
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 heme-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 [3,4,5].
Last update:December 2001 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Michel H. |
| Title | Cytochrome c oxidase: catalytic cycle and mechanisms of proton pumping--a discussion. | |
| Source | Biochemistry 38:15129-15140(1999). | |
| PubMed ID | 10563795 | |
| DOI | 10.1021/bi9910934 |
| 2 | Authors | Mather M.W. Springer P. Hensel S. Buse G. Fee J.A. |
| Title | Cytochrome oxidase genes from Thermus thermophilus. Nucleotide sequence of the fused gene and analysis of the deduced primary structures for subunits I and III of cytochrome caa3. | |
| Source | J. Biol. Chem. 268:5395-5408(1993). | |
| PubMed ID | 8383670 |
| 3 | Authors | Santana M. Kunst F. Hullo M.F. Rapoport G. Danchin A. Glaser P. |
| Title | Molecular cloning, sequencing, and physiological characterization of the qox operon from Bacillus subtilis encoding the aa3-600 quinol oxidase. | |
| Source | J. Biol. Chem. 267:10225-10231(1992). | |
| PubMed ID | 1316894 |
| 4 | Authors | Chepuri V. Lemieux L. Au D.C. Gennis R.B. |
| Title | The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases. | |
| Source | J. Biol. Chem. 265:11185-11192(1990). | |
| PubMed ID | 2162835 |
| 5 | Authors | Garcia-Horsman J.A. Barquera B. Rumbley J. Ma J. Gennis R.B. |
| Source | J. Bacteriol. 176:5587-5600(1994). |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)