10 research outputs found
Hyperfine Sublevel Correlation Spectroscopy Studies of Iron–Sulfur Cluster in Rieske Protein from Green Sulfur Bacterium Chlorobaculum tepidum
The magnetic properties
of the Rieske protein purified from Chlorobaculum tepidum were investigated using electron
paramagnetic resonance and hyperfine sublevel correlation spectroscopy
(HYSCORE). The <i>g</i>-values of the Fe<sub>2</sub>S<sub>2</sub> center were <i>g</i><sub><i>x</i></sub> = 1.81, <i>g</i><sub><i>y</i></sub> = 1.90,
and <i>g</i><sub><i>z</i></sub> = 2.03. Four classes
of nitrogen signals were obtained by HYSCORE. Nitrogens 1 and 2 had
relatively strong magnetic hyperfine couplings and were assigned as
the nitrogen directly ligated to Fe. Nitrogens 3 and 4 had relatively
weak magnetic hyperfine couplings and were assigned as the other nitrogen
of the His ligands and peptide nitrogen connected to the sulfur atom
via hydrogen bonding, respectively. The anisotropy of nitrogen 3 reflects
the different spin density distributions on the His ligands, which
influences the electron transfer to quinone