The N-Terminal Domain of Human DNA Helicase Rtel1 Contains a Redox Active Iron-Sulfur Cluster
Figure 3
Redox titration of the RtelN iron-sulfur cluster. (a) UV-visible spectra of purified RtelN. Purified RtelN (40 μM) (spectrum 1) was reduced with freshly prepared sodium dithionite (2 mM) (spectrum 2). (b) EPR spectra of purified RtelN. RtelN (90 μM) (spectrum 1) was reduced with freshly prepared sodium dithionite (2 mM) (spectrum 2). (c) Redox titration of purified RtelN. The amplitudes of the absorbance peak at 415 nm were normalized to 0 and 100% for the fully reduced and oxidized RtelN iron-sulfur cluster in solution, respectively. The solid line drawn through three sets of data points represents the best fit to a Nernst equation () with mV.
