Resonance Raman spectra of deoxyhemoproteins. Heme structure in relation to dioxygen binding
โ Scribed by A. Desbois; M. Lutz; R. Banerjee
- Book ID
- 118847121
- Publisher
- Elsevier Science
- Year
- 1981
- Weight
- 445 KB
- Volume
- 671
- Category
- Article
- ISSN
- 0005-2795
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๐ SIMILAR VOLUMES
Visible resonance Raman spectra in the low-frequency region (200-500 cm-') are reported for hemoglobin ( H b ) reconstituted with heme that is deuterated at the meso carbon atoms (meso-d,). Spectra were obtained in the deoxy form and in the immediate photoproduct of the carbonmonoxide adduct, HbCO.
The yield of quinoline-insoluble portion from pitches correlates well with the aromatic hydrogen content of the carbon disulphide-soluble fraction scaled up by proportion to the whole pitch, which therefore by implication is an indication of the binding properties. The chemical shifts are explained