Near-infrared magnetic circular dichroism of cytochrome c

• Published in: Biochemistry (Easton) Vol. 16; no. 8; pp. 1725 - 1729
• Main Authors: Rawlings, J, Stephens, P. J, Nafie, L. A, Kamen, M. D
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 19-04-1977
• Subjects: Chromatium - enzymology; Circular Dichroism; Cytochrome c Group - analogs & derivatives; Cytochromes c1; Magnetics; Oxidation-Reduction; Protein Conformation; Rhodopseudomonas - enzymology; Rhodospirillum rubrum - enzymology; Species Specificity; Spectrophotometry, Infrared
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi00627a032

The near-infrared magnetic circular dichroism (MCD) of Rhodospirillum rubrum, Chromatium vinosum, and Rhodopseudomonas palustris cytochromes c' are reported. The spectra of the reduced protein are very similar to those of deoxymyoglobin. The spectra of the oxidized proteins in the pD range 1-13 can be analyzed on the basis of four species A, B, C, and D. The existence of nine species, reported in a recent electron paramagnetic resonance study, is not substantiated. The MCD spectra support the assignment of B as high spin and C and D as low spin. The MCD of species A is close to that of high-spin proteins and does not support the recently proposed assignment of a mixed high- and intermediate-spin ground state for this species. The energies of the near-IR electronic transitions of all four oxidized species point to axial ligation via oxygen, assuming histidine to be the opposite axial ligand. Unfortunately, insufficient model compounds with ligation by carboxyl or hydroxyl moieties exist to enable more precise assignments.