An infrared study of nitric oxide bonding to heme B and hemoglobin A. Evidence for inositol hexaphosphate induced cleavage of proximal histidine to iron bonds
An infrared study of nitric oxide bonding to heme B and hemoglobin A. Evidence for inositol hexaphosphate induced cleavage of proximal histidine to iron bonds
复制标题
一氧化氮与血红素 B 和血红蛋白 A 结合的红外研究。六磷酸肌醇诱导近端组氨酸与铁键断裂的证据
DOI：
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发表时间：
1976
期刊：
影响因子：
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通讯作者：
W. Caughey
中科院分区：
文献类型：
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作者：
J. C. Maxwell;W. Caughey
合成了五配位和六配位亚硝基血红素，并测定了它们的红外光谱、电子顺磁共振(EPR)和可见光-索莱特光谱，并与亚硝基血红蛋白A(HBA-NO)在有无六磷酸肌醇(IHP)存在下的相应光谱进行了比较。由联吡啶和吡啶羰基原血红素二甲酯制备的五配位和六配位的NO络合物分别在1675和1625 cm-1附近有N-O拉伸带。这些频率对溶剂的变化很敏感(NUNO随着溶剂偶极矩的增加而减小)，对于六配位物种，对反式配体的变化很敏感。然而，与五配位和六配位物种之间的差异(约50 cm-11)相比，这些溶剂和反式配体的影响很小。反式配体的性质影响了两者的相对比例。
Five- and six-coordinate nitrosyl hemes have been prepared and their infrared, electron paramagnetic resonance (EPR), and visible-Soret spectra compared with the corresponding spectra for nitrosyl hemoglobin A (Hba-NO) determined both in the presence and the absence of inositol hexaphosphate (IHP). The five- and six-coordinate NO complexes prepared from either dipyridine or pyridine carbonyl protoheme dimethyl ester had N-O stretch bands (nuno) near 1675 and 1625 cm-1, respectively. These frequencies are sensitive to change in solvent (nuno decreased as the dipole moment of the solvent increased) and, with six-coordinate species, to changes in trans ligand. However, these solvent and trans ligand effects were small compared with the difference (ca. 50 cm-11) between five- and six -coordinate species. The nature of the trans ligand affected the relative proportions of the two...