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• W2085476503 endingPage "214" @default.
• W2085476503 startingPage "202" @default.
• W2085476503 abstract "1. CD spectra of cytochrome c oxidase have been determined both in the absence and presence of the extrinsic ligands CO, NO, cyanide and azide.2. CO and NO affect the CD spectrum of cytochrome c oxidase in a similar way.3. Cyanide and azide also affect the CD spectrum of cytochrome c oxidase in a similar way, but distinctly different from CO and NO.4. From the CD spectra of the oxidized and reduced enzyme, in the presence and absence of extrinsic ligands, CD difference spectra (reduced minus oxidized) are calculated for the so-called cytochrome a and cytochrome a3 moieties of the enzyme.5. These spectra are largely dependent on the extrinsic ligand used. It is therefore concluded that these spectra do not represent independent cytochrome a and cytochrome a3 difference spectra, but that heme-heme interactions occur within the cytochrome c oxidase molecule, in such a way that binding of a ligand to one of the heme a groups of cytochrome c oxidase affects the spectral properties of the other heme a group.6. As a consequence, ligand-binding studies cannot give information as to the pre-existence of separate cytochrome a and cytochrome a3 moieties in the absence of extrinsic ligands." @default.
• W2085476503 created "2016-06-24" @default.
• W2085476503 creator A5031982800 @default.
• W2085476503 creator A5040093604 @default.
• W2085476503 date "1974-05-01" @default.
• W2085476503 modified "2023-09-26" @default.
• W2085476503 title "Biochemical and biophysical studies on cytochrome c oxidase XVI. Circular dichroic study of cytochrome c oxidase and its ligand complexes" @default.
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• W2085476503 doi "https://doi.org/10.1016/0005-2728(74)90045-0" @default.
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