Pub. Date : 1993 Jan 12
PMID : 8380332
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Fourier-transform infrared study of azide binding to the Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: new evidence for a redox-linked conformational change at the binuclear site. | Azides | cytochrome c oxidase subunit 6A1, mitochondrial | Bos taurus |
| 2 | Azide binding to the Fea3-CuB site of cytochrome c oxidase purified from bovine heart mitochondria was investigated in various redox levels by Fourier-transform infrared spectroscopy. | Azides | cytochrome c oxidase subunit 6A1, mitochondrial | Bos taurus |
| 3 | Upon addition of cyanide to the preformed fully oxidized cytochrome c oxidase-azide complex, a new azide species exhibiting a sharp antisymmetric stretching band at 2032.5 cm-1 was formed. | Azides | cytochrome c oxidase subunit 6A1, mitochondrial | Bos taurus |
| 4 | Upon addition of cyanide to the preformed fully oxidized cytochrome c oxidase-azide complex, a new azide species exhibiting a sharp antisymmetric stretching band at 2032.5 cm-1 was formed. | Azides | cytochrome c oxidase subunit 6A1, mitochondrial | Bos taurus |
| 5 | This cytochrome c oxidase-azide-cyanide ternary complex is relatively stable, and cyanide ion replaces the 2032.5-cm-1 azide species very slowly, resulting in the formation of the Fea3(3+)-C-N-CuB2+ bridging structure characterized by the 2152-cm-1 band. | Azides | cytochrome c oxidase subunit 6A1, mitochondrial | Bos taurus |
| 6 | Upon the introduction of 1 electron equivalent to the fully oxidized cytochrome c oxidase-azide complex, an azide band at 2003.5 cm-1 developed. | Azides | cytochrome c oxidase subunit 6A1, mitochondrial | Bos taurus |
| 7 | Upon the introduction of 1 electron equivalent to the fully oxidized cytochrome c oxidase-azide complex, an azide band at 2003.5 cm-1 developed. | Azides | cytochrome c oxidase subunit 6A1, mitochondrial | Bos taurus |