Structural characterization of isolated mitochondrial cytochrome c1.
Resonance Raman spectroscopy (RRS) has been employed to characterize cytochromes c1 isolated from bc1 complexes of beef heart mitochondria and Rhodopseudomonas sphaeroides. The data obtained in this study extend the physical characterization of cytochromes c1 and focus on the effects of the local protein environment on the heme active site. While the general characteristics of the cytochromes c1 are similar to those of smaller soluble cytochromes c, the behavior of several core-size and ligation-sensitive heme modes reveal that significant systematic differences exist between those species. These, most likely, result from changes in the heme axial-ligand interactions.
Department of Chemistry, University of New Mexico, Albuquerque 87131.
B S
BS
Lou
J D
JD
Hobbs
Y R
YR
Chen
L
L
Yu
C A
CA
Yu
M R
MR
Ondrias
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003575:Cytochromes c1 / Q000737:chemistry*; D006418:Heme / Q000737:chemistry; D008929:Mitochondria, Heart / Q000201:enzymology*; D010084:Oxidation-Reduction; D012242:Rhodobacter sphaeroides / Q000201:enzymology; D013059:Spectrum Analysis, Raman
D006418:Heme; D003575:Cytochromes c1