Bonding in HNO-myoglobin as characterized by X-ray absorption and resonance Raman spectroscopies
Bonding in HNO-myoglobin as characterized by X-ray absorption and resonance Raman spectroscopies
复制标题
DOI：
10.1021/ja0433727
复制
发表时间：
2005-01-26
影响因子：
15
通讯作者：
Lay, PA
中科院分区：
文献类型：
--
作者：
Immoos, CE;Sulc, F;Lay, PA
HNO-肌红蛋白加合物1的EXAFS和共振拉曼光谱与HNO与血红素中心结合的存在是一致的。通过对血红素蛋白EXAFs的多重散射(MS)分析得到了1的三维结构，得到了Fe−N−O键角为13 1°，Fe−N键长为1 82？，与已发表的含RNO配体的模型络合物的结果相吻合.共振拉曼光谱确定了ν(NO)在1385 cm~(-1)处的伸展(由15N标记证实)，这与报道的小分子HNO络合物的结果很好地一致。ν(Fe−N)在636 cm~(-1)处的波长显著高于MBIINO和MbIIINO的波长(分别为554和595 cm-1)。XAFS、XANES和共振拉曼光谱数据都与从核磁共振实验中推导出的结构一致，为HNO与金属中心之间的成键提供了更详细的信息。
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 of1obtained from multiple-scattering (MS) analysis of the EXAFS of the heme protein yielded an Fe−N−O bond angle of 131° and an Fe−N bond length of 1.82 Å, which compare well with published values for model complexes containing RNO ligands. Resonance Raman spectra identified the ν(NO) stretch at 1385 cm-1(confirmed by15N labeling), which corresponds well with those reported for small molecule HNO complexes. The wavelength of the ν(Fe−N) at 636 cm-1of1is 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.