AbstractAddition of cyanide to the CO complex of cytochrome oxidase reduces the apparent photosensitivity of the FeCO bond. This effect is not seen with azide, or when cyanide is added to ferromyoglobin-CO. It is proposed that cyanide binds to CuB, and restricts the passage of CO out of the protein. This restriction favors geminate recombination of CO and ferrocytochrome a3, thereby lowering the apparent quantum yield for CO photolysis. The apparent Kd of cyanide for CuB is 15.4 mM. These data support a direct role for CuB in ligand binding by cytochrome c oxidase
Knowledge of the mechanism of O2 reduction and ligand access in heme-copper oxidases is essential fo...
AbstractX-ray structures of bovine heart cytochrome c oxidase with bound respiratory inhibitors (O2 ...
AbstractThe rate of formation of the mixed-valence state of cytochrome c oxidase on incubation with ...
AbstractAddition of cyanide to the CO complex of cytochrome oxidase reduces the apparent photosensit...
AbstractPhotodissociation of the fully reduced carbonmonoxy bound cytochrome aa3 from Rb. sphaeroide...
The route of O₂to and from the high-spin heme in heme-copper oxidases has generally been believed to...
AbstractThe route of O2 to and from the high-spin heme in heme–copper oxidases has generally been be...
Nanosecond time-resolved magnetic circular dichroism (TRMCD) and time-resolved natural circular dich...
(1) R.H. Austin, K.W. Beeson, L. Eisenstein, H. Frauenfelder, and I.C. Gunsalus (1975) Biochemistry ...
Cytochrome c oxidase (CcO), the terminal enzyme in the mitochondrial respiratory chain, catalyzes th...
AbstractSmall increases in NO concentration can inhibit mitochondrial oxygen consumption by reacting...
Abstract We present novel experimental evidence that, starting with the oxidized enzyme, the interna...
Contrary to most heme proteins, ferrous cytochrome c does not bind ligands such as cyanide and CO. I...
AbstractThe slow increase of a cyanide-induced optical change at 437 nm following rapid cyanide inhi...
Novel experimental evidence is presented further supporting the hypothesis that, starting with resti...
Knowledge of the mechanism of O2 reduction and ligand access in heme-copper oxidases is essential fo...
AbstractX-ray structures of bovine heart cytochrome c oxidase with bound respiratory inhibitors (O2 ...
AbstractThe rate of formation of the mixed-valence state of cytochrome c oxidase on incubation with ...
AbstractAddition of cyanide to the CO complex of cytochrome oxidase reduces the apparent photosensit...
AbstractPhotodissociation of the fully reduced carbonmonoxy bound cytochrome aa3 from Rb. sphaeroide...
The route of O₂to and from the high-spin heme in heme-copper oxidases has generally been believed to...
AbstractThe route of O2 to and from the high-spin heme in heme–copper oxidases has generally been be...
Nanosecond time-resolved magnetic circular dichroism (TRMCD) and time-resolved natural circular dich...
(1) R.H. Austin, K.W. Beeson, L. Eisenstein, H. Frauenfelder, and I.C. Gunsalus (1975) Biochemistry ...
Cytochrome c oxidase (CcO), the terminal enzyme in the mitochondrial respiratory chain, catalyzes th...
AbstractSmall increases in NO concentration can inhibit mitochondrial oxygen consumption by reacting...
Abstract We present novel experimental evidence that, starting with the oxidized enzyme, the interna...
Contrary to most heme proteins, ferrous cytochrome c does not bind ligands such as cyanide and CO. I...
AbstractThe slow increase of a cyanide-induced optical change at 437 nm following rapid cyanide inhi...
Novel experimental evidence is presented further supporting the hypothesis that, starting with resti...
Knowledge of the mechanism of O2 reduction and ligand access in heme-copper oxidases is essential fo...
AbstractX-ray structures of bovine heart cytochrome c oxidase with bound respiratory inhibitors (O2 ...
AbstractThe rate of formation of the mixed-valence state of cytochrome c oxidase on incubation with ...