. Author manuscript; available in PMC: 2012 May 17.

Published in final edited form as: Biochemistry. 2011 Apr 22;50(19):3957–3967. doi: 10.1021/bi1020748

Table 1. Values for the K_d’s determined for the interactions between the CYP2B4-FM variants on the proximal side of the protein and CPR by fluorescence titration.

CYP2B4-FM variant	K_d
(L420C)FM	0.13±0.02
(L270C)FM	0.68±0.09
(R133C)FM	0.49±0.05
(V267C)FM	0.73±0.07

The fluorescence emission of the 0.05 µM CYP2B4FM proximal variants were recorded in the presence of 0.1 mg/ml DLPC and 50 mM potassium phosphate, pH 7.4, at 22 ° C. The CYP2B4FM samples were then reconstituted with increasing concentrations of CPR. The resulting titration curves were fit to the Michaelis-Menten equation from which K_d’s were determined.

Table 1. Values for the Kd’s determined for the interactions between the CYP2B4-FM variants on the proximal side of the protein and CPR by fluorescence titration.

Table 1. Values for the K_d’s determined for the interactions between the CYP2B4-FM variants on the proximal side of the protein and CPR by fluorescence titration.