Biochemical and Biophysical Research Communications, Vol.450, No.1, 25-29, 2014
The Fe-heme structure of met-indoleamine 2,3-dioxygenase-2 determined by X-ray absorption fine structure
Multiple-scattering (MS) analysis of EXAFS data on met-indoleamine 2,3-dioxygenase-2 (IDO2) and analysis of XANES have provided the first direct structural information about the axial donor ligands of the iron center for this recently discovered protein. At 10 K, it exists in a low-spin bis(His) form with Fe-N-p(av) = 1.97 angstrom, the Fe-N-Im bond lengths of 2.11 angstrom and 2.05 angstrom, which is in equilibrium with a high-spin form at room temperature. The bond distances in the low-spin form are consistent with other low-spin hemeproteins, as is the XANES spectrum, which is closer to that of the low-spin met-Lb than that of the high-spin met-Mb. The potential physiological role of this spin equilibrium is discussed. (C) 2014 Elsevier Inc. All rights reserved.
Keywords:Indoleamine 2,3-dioxygenase-2 (IDO2);X-ray absorption fine structure;EXAFS;Home environment;Mixed-spin species