Comparative Raman studies of cytochrome b562 and cytochrome c
β Scribed by R. B. Srivastava; C. Pace; Nai-Teng Yu
- Publisher
- John Wiley and Sons
- Year
- 1981
- Tongue
- English
- Weight
- 450 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0377-0486
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Resonance Raman studies of three mutants of cytochrome c demonstrated the sensitivity of the spectra to mutations that a β ect the interactions of the heme peripheral substituents with the protein matrix. The most dramatic di β erences in the spectra of the reduced mutant cytochromes, as compared with
The UV-visible, circular dichroism (CD), and resonance Raman (RR) spectra of the wild type yeast iso-1-cytochrome c (WT) and its mutant F82H in which phenylalanine-82 (Phe-82) is substituted with His are measured and compared for oxidized and reduced forms. The CD spectra in the intrinsic and Soret