Effect of charge interactions on the carboxylate vibrational stretching frequency in c-type cytochromes investigated by continuum electrostatic calculations and FTIR spectroscopy.
The FTIR spectra of the asymmetric carboxylate absorption region of three c-type cytochromes--namely horse heart, yeast and bonito cytochromes c--as well as continuum electrostatic calculations performed on their respective protein matrices, show that these combined methods can target specific protein regions and yield pertinent protein charge information that correlates with the observed spectral data. Deconvolution of the IR carboxylate stretch frequency region (1525-1675 cm-1) in the three cytochromes yield different v(oco)a distributions. In the case of the bonito cytochrome c carboxylates, two v(oco)a populations are clearly distinguishable in the deconvoluted spectra--which is not the case for the more complex v(oco)a deconvolutions of the other two cytochromes. The frequency distributions of the calculated potentials are consistent with the experimental observations and we conclude that the IR carboxylate absorption in proteins can be modified by the electrostatic environment.
Laberge
M
M
Johnson Research Foundation, Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia 19104, USA. labergem@mail.med.upenn.edu
Sharp
K A
KA
Vanderkooi
J M
JM
D000818:Animals; D002264:Carboxylic Acids / Q000737:chemistry*; D003574:Cytochrome c Group / Q000737:chemistry*; D004563:Electrochemistry; D005399:Fishes; D006860:Hydrogen Bonding; D008958:Models, Molecular; D009206:Myocardium / Q000201:enzymology; D016012:Poisson Distribution; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared; D017550:Spectroscopy, Fourier Transform Infrared; D015003:Yeasts / Q000201:enzymology
D002264:Carboxylic Acids; D003574:Cytochrome c Group