Title : 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.

Pub. Date : 1993 Jan 12

PMID : 8380332






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 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. Cyanides cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus
2 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. Cyanides cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus
3 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. Cyanides cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus