The 2.03 signal as an indicator of dinitrosyl-iron complexes with thiol-containing ligands.

The parameters of EPR signal from dinitrosyl-iron complexes (DNIC) with bovine serum albumin (BSA), horse hemoglobin (Hb), and apometallothionein (apo-Mt) of horse kidney incorporating one (BSA, Hb) or two thiol-containing ligands (apo-Mt) were compared. The EPR signal from DNIC-BSA was characterized by the rhombic symmetry of g tensor at room temperature of signal recording (ambient temperature) or at 77K in the solution frozen in the presence of glycerol. In freezing of the solution in the absence of glycerin, under the exposure of DNIC-BSA to negatively charged sodium dodecyl sulfate (SDS) ions, or in the incorporation of DNIC-BSA into the reversed micelles formed by negatively charged ions of surfactant aerosol OT, the symmetry of the g tensor of DNIC-BSA EPR signal increased to axial. A similarly high symmetry of g tensor was observed for the DNIC-Hb EPR signal in the absence of any influence on this protein complex. The shape of EPR signals from these preparations recorded at 77K was identical to that of EPR signal from DNIC with cysteine in frozen solution. In this connection it was concluded that the EPR signal from this low-molecular DNIC with the (RS-)2Fe+(NO+)2 structure cannot be considered as a peculiar "fingerprint" of DNIC with the same structure in biosystems. In such systems the same signal can originate from protein DNIC incorporating only one thiol-containing ligand along with a nonthiol ligand. The EPR signal displayed by DNIC with apo-Mt with a high content of cysteine residues at room temperature of registration was identical to the EPR signal from frozen solution of DNIC with cysteine. This protein DNIC is apparently characterized by the same structure as DNIC with cysteine.