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Raman difference spectra have been obtained for the cytochromes c of a number of species by simultaneous data acquisition from two samples. Frequency differences as small as 0.1 cm-1 can be measured reproducibly by the technique we have developed. In comparisons between cytochromes c isolated from two different species, the frequency differences in the heme vibrational modes range from 0 to 6 cm-1. The vibrational frequencies of the heme are sensitive to the electronic charge density on the porphyrin macrocycle. The frequency differences are interpreted in terms of the influence of the heme-packed aromatic and highly electronegative amino acid side chains on the pi* charge density and distribution on the heme. Such a control of the electronic properties of the heme by the protein may be important for the function of cytochrome c.
J A Shelnutt, and
D L Rousseau, and
J K Dethmers, and
E Margoliashi
February 1983,
The Journal of biological chemistry,
J A Shelnutt, and
D L Rousseau, and
J K Dethmers, and
E Margoliashi
June 1974,
Biochimica et biophysica acta,
J A Shelnutt, and
D L Rousseau, and
J K Dethmers, and
E Margoliashi
September 1986,
Biochimica et biophysica acta,
J A Shelnutt, and
D L Rousseau, and
J K Dethmers, and
E Margoliashi
February 2000,
Biochemistry,
J A Shelnutt, and
D L Rousseau, and
J K Dethmers, and
E Margoliashi
May 1998,
Biochemistry,
J A Shelnutt, and
D L Rousseau, and
J K Dethmers, and
E Margoliashi
August 1965,
Proceedings of the National Academy of Sciences of the United States of America,
J A Shelnutt, and
D L Rousseau, and
J K Dethmers, and
E Margoliashi
February 1986,
The Journal of biological chemistry,
J A Shelnutt, and
D L Rousseau, and
J K Dethmers, and
E Margoliashi
July 1993,
Biochemistry,
J A Shelnutt, and
D L Rousseau, and
J K Dethmers, and
E Margoliashi
July 1988,
Biochemistry,
J A Shelnutt, and
D L Rousseau, and
J K Dethmers, and
E Margoliashi
February 1982,
FEBS letters,
