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Resonance Raman study of cytochrome c water mutants

✍ Scribed by Chengli Zhou; Junwei Zheng; Abel Schejter; Wenying Qin; Emanuel Margoliash; Therese M. Cotton

Publisher: John Wiley and Sons
Year: 1998
Tongue: English
Weight: 322 KB
Volume: 29
Category: Article
ISSN: 0377-0486
DOI: 10.1002/(sici)1097-4555(199810/11)29:10/11<955::aid-jrs324>3.0.co;2-v

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✦ Synopsis

Resonance Raman studies of three mutants of cytochrome c demonstrated the sensitivity of the spectra to mutations that a †ect the interactions of the heme peripheral substituents with the protein matrix. The most dramatic di †erences in the spectra of the reduced mutant cytochromes, as compared with that of wild-type cytochrome c, are observed in the low-wavenumber region of the reduced proteins. The bands that are most strongly a †ected include bending modes of the thioether linkages and propionic acid side-chains. These modes are activated by the distortion of saddling of the heme macrocycle in the protein pocket. The high-wavenumber spectral region of the mutants is nearly identical with that of the wild type. The spectral changes are less pronounced in the oxidized form of the mutant cytochromes. This observation is consistent with the more open structure of ferricytochrome c than ferrocytochrome c.

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