CW-EPR and ENDOR study of cytochrome c6 from Anabaena PCC 7119.
The detailed analysis of the continuous-wave electron paramagnetic resonance and electron nuclear double resonance measurements on cytochrome c(6) from Anabaena PCC7119 reveals several electronic and structural properties of this hemeprotein. The oxidized protein shows two forms that differ in the arrangement of the residues that act as heme axial ligands. Information about the orientation of these residues is obtained for one of the forms, which turns out to differ from that found in the reduced protein from x-ray experiments. The biological significance of these results is discussed.
García-Rubio
Inés
I
Instituto de Ciencia de Materiales de Aragón, CSIC-Universidad de Zaragoza, C/Pedro Cerbuna 12, E-50009 Zaragoza, Spain.
Medina
Milagros
M
Cammack
Richard
R
Alonso
Pablo J
PJ
Martínez
Jesús I
JI
D017033:Anabaena / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D003198:Computer Simulation; D045365:Cytochromes c6 / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D020033:Protein Isoforms / Q000737:chemistry
D001426:Bacterial Proteins; D045365:Cytochromes c6; D020033:Protein Isoforms