Immoos Chad E, Sulc Filip, Farmer Patrick J, Czarnecki Kazimierz, Bocian David F, Levina Aviva, Aitken Jade B, Armstrong Robert S, Lay Peter A
Department of Chemistry, University of California, Irvine, California 92697-2025, USA.
J Am Chem Soc. 2005 Jan 26;127(3):814-5. doi: 10.1021/ja0433727.
The EXAFS and resonance Raman spectra on the HNO-myoglobin adduct, 1, are consistent with the presence of HNO bound to a heme center. The three-dimensional structure about the heme center of 1 obtained from multiple-scattering (MS) analysis of the EXAFS of the heme protein yielded an Fe-N-O bond angle of 131 degrees and an Fe-N bond length of 1.82 A, which compare well with published values for model complexes containing RNO ligands. Resonance Raman spectra identified the nu(N=O) stretch at 1385 cm-1 (confirmed by 15N labeling), which corresponds well with those reported for small molecule HNO complexes. The wavelength of the nu(Fe-N) at 636 cm-1 of 1 is significantly higher than those of MbIINO and MbIIINO (554 and 595 cm-1, respectively). The XAFS, XANES, and resonance Raman data are all consistent with the structure deduced from the NMR experiments, providing more detail on the bonding between HNO and the metal center.
HNO-肌红蛋白加合物1的扩展X射线吸收精细结构（EXAFS）和共振拉曼光谱与结合在血红素中心的HNO的存在一致。通过对血红素蛋白的EXAFS进行多重散射（MS）分析得到的1的血红素中心的三维结构，其Fe-N-O键角为131度，Fe-N键长为1.82 Å，这与含有RNO配体的模型配合物的已发表值相当吻合。共振拉曼光谱确定在1385 cm-1处有ν(N=O)伸缩振动（通过15N标记确认），这与报道的小分子HNO配合物的情况相当吻合。1在636 cm-1处的ν(Fe-N)波长明显高于MbIINO和MbIIINO的（分别为554和595 cm-1）。XAFS、XANES和共振拉曼数据都与从NMR实验推导的结构一致，提供了关于HNO与金属中心之间键合的更多细节。
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