1OCZ
BOVINE HEART CYTOCHROME C OXIDASE IN AZIDE-BOUND STATE
Summary for 1OCZ
| Entry DOI | 10.2210/pdb1ocz/pdb |
| Descriptor | CYTOCHROME C OXIDASE, COPPER (II) ION, MAGNESIUM ION, ... (19 entities in total) |
| Functional Keywords | oxidoreductase (cytochrome(c)-oxygen), cytochrome c oxidase, azide-bound, oxidoreductase |
| Biological source | Bos taurus (cattle) More |
| Cellular location | Mitochondrion inner membrane; Multi-pass membrane protein: P00396 P68530 P00415 Mitochondrion inner membrane: P07470 P13183 P00430 P10175 P00423 P00426 P00428 P07471 P04038 Mitochondrion intermembrane space: P00429 |
| Total number of polymer chains | 26 |
| Total formula weight | 413823.33 |
| Authors | Tsukihara, T.,Yao, M. (deposition date: 1998-07-13, release date: 1999-07-22, Last modification date: 2024-12-25) |
| Primary citation | Yoshikawa, S.,Shinzawa-Itoh, K.,Nakashima, R.,Yaono, R.,Yamashita, E.,Inoue, N.,Yao, M.,Fei, M.J.,Libeu, C.P.,Mizushima, T.,Yamaguchi, H.,Tomizaki, T.,Tsukihara, T. Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase. Science, 280:1723-1729, 1998 Cited by PubMed Abstract: Crystal structures of bovine heart cytochrome c oxidase in the fully oxidized, fully reduced, azide-bound, and carbon monoxide-bound states were determined at 2.30, 2.35, 2.9, and 2.8 angstrom resolution, respectively. An aspartate residue apart from the O2 reduction site exchanges its effective accessibility to the matrix aqueous phase for one to the cytosolic phase concomitantly with a significant decrease in the pK of its carboxyl group, on reduction of the metal sites. The movement indicates the aspartate as the proton pumping site. A tyrosine acidified by a covalently linked imidazole nitrogen is a possible proton donor for the O2 reduction by the enzyme. PubMed: 9624044DOI: 10.1126/science.280.5370.1723 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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