Domain motion in cytochrome P450 reductase: conformational equilibria revealed by NMR and small-angle x-ray scattering.

6 In the crystal structure, the ε-amino group of Lys 75 is within hydrogen-bonding distance of the carboxylate of Glu 354 , a residue on a loop of the linker domain; however, these residues are essentially completely solvent-exposed, and this interaction may not be significant in solution. 7 The 4-electron reduced species may not be physiologically relevant ( 45 ), but it represents a stable reduced state of the enzyme that can conveniently be studied under the conditions of the SAXS experiment. 8 The accuracy of the EOM is determined by the extent to which the large pool of structures it generates provides an adequate portrayal of all the potential conformers and by the procedure of the filtering process ( 43 ).

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