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- W1567482940 abstract "Abstract The exposure of the heme moiety of cytochrome c to various solvents was investigated by the technique of solvent perturbation. The heme hexadecapeptide in a chymotryptic digest of the protein was used as a model compound for the fully exposed chromophore. While the Soret absorption of both ferri- and ferrocytochrome c was enhanced in 20% ethylene glycol, the extent of enhancement, Δe/e, was substantially less than that measured for the model compound or for the unfolded protein in 8 m urea. The percentage maximal perturbation of ferrocytochrome c was found to be independent of the radius of the perturbant over the range from 1.4 to 3.6 A. It was concluded that only a portion of the heme moiety of native cytochrome c is in contact with the solvent. Replacement of one of the two protein-heme coordinate-covalent bonds by cyanide increased the exposure of the heme to the solvent." @default.
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- W1567482940 date "1967-02-01" @default.
- W1567482940 modified "2023-10-14" @default.
- W1567482940 title "Location of the Heme Moiety of Cytochrome c by Solvent Perturbation" @default.
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- W1567482940 doi "https://doi.org/10.1016/s0021-9258(18)96247-2" @default.
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