PMID- 24858687 OWN - NLM STAT- MEDLINE DCOM- 20140921 LR - 20211108 IS - 1090-2104 (Electronic) IS - 0006-291X (Linking) VI - 450 IP - 1 DP - 2014 Jul 18 TI - The Fe-heme structure of met-indoleamine 2,3-dioxygenase-2 determined by X-ray absorption fine structure. PG - 25-9 LID - S0006-291X(14)00926-7 [pii] LID - 10.1016/j.bbrc.2014.05.054 [doi] AB - 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 10K, it exists in a low-spin bis(His) form with Fe-Np(av)=1.97A, the Fe-NIm bond lengths of 2.11A and 2.05A, 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. CI - Copyright (c) 2014 Elsevier Inc. All rights reserved. FAU - Aitken, Jade B AU - Aitken JB AD - School of Chemistry, The University of Sydney, NSW 2006, Australia; Australian Synchrotron, Clayton, Victoria 3168, Australia; Institute of Materials Structure Science, KEK, Tsukuba, Ibaraki 305-0801, Japan. FAU - Austin, Christopher J D AU - Austin CJ AD - School of Chemistry, The University of Sydney, NSW 2006, Australia; Department of Pathology and Bosch Institute, The University of Sydney, Camperdown, NSW 2006, Australia. FAU - Hunt, Nicholas H AU - Hunt NH AD - Department of Pathology and Bosch Institute, The University of Sydney, Camperdown, NSW 2006, Australia. FAU - Ball, Helen J AU - Ball HJ AD - Department of Pathology and Bosch Institute, The University of Sydney, Camperdown, NSW 2006, Australia. FAU - Lay, Peter A AU - Lay PA AD - School of Chemistry, The University of Sydney, NSW 2006, Australia. Electronic address: peter.lay@sydney.edu.au. LA - eng GR - P41RR001209/RR/NCRR NIH HHS/United States PT - Journal Article PT - Research Support, N.I.H., Extramural PT - Research Support, Non-U.S. Gov't PT - Research Support, U.S. Gov't, Non-P.H.S. DEP - 20140522 PL - United States TA - Biochem Biophys Res Commun JT - Biochemical and biophysical research communications JID - 0372516 RN - 0 (IDO2 protein, human) RN - 0 (Indoleamine-Pyrrole 2,3,-Dioxygenase) RN - 42VZT0U6YR (Heme) RN - E1UOL152H7 (Iron) SB - IM MH - Computer Simulation MH - Heme/*chemistry MH - Indoleamine-Pyrrole 2,3,-Dioxygenase/*chemistry/*ultrastructure MH - Iron/*chemistry MH - *Models, Chemical MH - *Models, Molecular MH - Protein Conformation OTO - NOTNLM OT - EXAFS OT - Heme environment OT - Indoleamine 2,3-dioxygenase-2 (IDO2) OT - Mixed-spin species OT - X-ray absorption fine structure EDAT- 2014/05/27 06:00 MHDA- 2014/09/23 06:00 CRDT- 2014/05/27 06:00 PHST- 2014/05/07 00:00 [received] PHST- 2014/05/14 00:00 [accepted] PHST- 2014/05/27 06:00 [entrez] PHST- 2014/05/27 06:00 [pubmed] PHST- 2014/09/23 06:00 [medline] AID - S0006-291X(14)00926-7 [pii] AID - 10.1016/j.bbrc.2014.05.054 [doi] PST - ppublish SO - Biochem Biophys Res Commun. 2014 Jul 18;450(1):25-9. doi: 10.1016/j.bbrc.2014.05.054. Epub 2014 May 22.