Abstract
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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
