PMID- 21894911 OWN - NLM STAT- MEDLINE DCOM- 20120316 LR - 20221207 IS - 1520-510X (Electronic) IS - 0020-1669 (Linking) VI - 50 IP - 19 DP - 2011 Oct 3 TI - Ligand binding intermediates of nitrosylated human hemoglobin induced at low temperature by X-ray irradiation. PG - 9423-9 LID - 10.1021/ic201086u [doi] AB - Under prolonged X-ray irradiation, the ferrous heme of nitrosylated human adult hemoglobin derivative (HbNO) undergoes a reversible transition generating a 5-coordinate species, due to release of the Fe-NO bond. The overall process can be investigated using X-ray absorption near edge structure (XANES) spectroscopy. In this work, Fe K-edge XANES spectra were measured at T < 15 K, pH 9.2, i.e., on a high-affinity state (R-HbNO) where all the hemes are 6-coordinate, and at pH 6.5 in the presence of inositol hexakis-phosphate (IHP), i.e., on a low-affinity ligated state (T-HbNO) where the iron-hemes of the alpha-chains are 5-coordinate due to breaking of the Fe-proximal histidine bond. Under X-ray irradiation, 5-coordinate Fe-hemes are populated in both R-HbNO and T-HbNO, the Fe-NO bond lysis induced in T-HbNO involving rebinding of the proximal histidine to the transiently populated 4-coordinate hemes of the alpha-chains. A detailed analysis of the spectra confirms that different intermediate states in the ligand binding cooperative process of hemoglobin can be populated by X-ray irradiation, and that the part of the energy associated to the R-T quaternary transition, that is transmitted to the heme site, can be monitored by XANES spectroscopy. FAU - Arcovito, Alessandro AU - Arcovito A AD - Istituto di Biochimica e Biochimica Clinica, Universita Cattolica del Sacro Cuore, Largo F. Vito 1,00168, Roma, Italy. alessandro.arcovito@rm.unicatt.it FAU - Della Longa, Stefano AU - Della Longa S LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't DEP - 20110830 PL - United States TA - Inorg Chem JT - Inorganic chemistry JID - 0366543 RN - 0 (Glycated Hemoglobin A) RN - 0 (hemoglobin A, glycosylated-nitric oxide complex) RN - 31C4KY9ESH (Nitric Oxide) RN - E1UOL152H7 (Iron) SB - IM MH - Cold Temperature MH - Glycated Hemoglobin/*chemistry MH - Humans MH - Iron/*chemistry MH - Kinetics MH - Nitric Oxide/*chemistry MH - Protein Conformation MH - X-Ray Absorption Spectroscopy EDAT- 2011/09/08 06:00 MHDA- 2012/03/17 06:00 CRDT- 2011/09/08 06:00 PHST- 2011/09/08 06:00 [entrez] PHST- 2011/09/08 06:00 [pubmed] PHST- 2012/03/17 06:00 [medline] AID - 10.1021/ic201086u [doi] PST - ppublish SO - Inorg Chem. 2011 Oct 3;50(19):9423-9. doi: 10.1021/ic201086u. Epub 2011 Aug 30.