Fe(TPP)((13)CO)(NMeIm) | 934736-92-2

• 英文名称: Fe(TPP)((13)CO)(NMeIm)
• 英文别名: (N-MeIm)Fe(II)(TPP)((13)CO)
• CAS: 934736-92-2
• 化学式: C₄₉H₃₄FeN₆O
• 分子量: 779.685
• InChiKey: AYHSFCIDAOWNBN-GADWLLQISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  None
• 重原子数：
  None
• 可旋转键数：
  None
• 环数：
  None
• sp3杂化的碳原子比例：
  None
• 拓扑面积：
  None
• 氢给体数：
  None
• 氢受体数：
  None

反应信息

• 作为产物：
  描述：

  [Fe(meso-tetraphenylporphyrin)(CO)(1-methylimidazole)] 、 C13取代的一氧化碳 在 catalyst: 10percent Pd on Al₂O₃ 作用下， 以 正庚烷 为溶剂， 生成 Fe(TPP)((13)CO)(NMeIm)
  参考文献：
  名称：

  An Experimental and Quantum Chemical Investigation of CO Binding to Heme Proteins and Model Systems:  A Unified Model Based on ¹³C, ¹⁷O, and ⁵⁷Fe Nuclear Magnetic Resonance and ⁵⁷Fe Mössbauer and Infrared Spectroscopies

  摘要：

  We have investigated the question of how CO ligands bind to iron in metalloporphyrins and metalloproteins by using a combination of nuclear magnetic resonance (NMR), Fe-57 Mossbauer, and infrared spectroscopic techniques, combined with density functional theoretical calculations to analyze the spectroscopic results. The results of C-13 NMR isotropic chemical shift, C-13 NMR chemical shift anisotropy, O-17 NMR isotropic chemical shift, O-17 nuclear quadrupole coupling constant, Fe-57 MMR isotropic chemical shift, Fe-57 Mossbauer quadrupolar splitting, and infrared measurements indicate that CO binds to Fe in a close to linear fashion in all conformational substates. The C-13-isotropic shift and shift anisotropy for an A(0) substate model compound: Fe(5,10,15,20-tetraphenylporphyrin)(CO)(N-methylimidazole), as well as the O-17 chemical shift, and the O-17 nuclear quadrupole coupling constant (NQCC) are virtually the same as those found in the A(0) substate of Physeter catodon CO myoglobin and lead to most probable ligand tilt (tau) and bend (beta) angles of 0 degrees and 1 degrees when using a Bayesian probability or Z surface method fur structure determination. The infrared vco for the model compound of 1969 cm(-1) is also that found for A(0) proteins. Results for the A(1) substate (including the Fe-57 NMR chemical shift and Mossbauer quadrupole splitting) are also consistent with close to linear and untilted Fe-C-O geometries (tau = 4 degrees, P = 7 degrees), with the small changes in ligand spectroscopic parameters being attributed to electrostatic field effects. When taken together, the C-13 shift, C-13 shift anisotropy, O-17 shift, O-17 NQCC, Fe-57 shift, Fe-57 Mossbauer quadrupole splitting, and nu(CO) all strongly indicate very close to linear and untilted Fe-C-O geometries for all carbonmonoxyheme proteins. These results represent the first detailed quantum chemical analysis of metal-ligand geometries in metalloproteins using up to seven different spectroscopic observables from three types of spectroscopy and suggest a generalized approach to structure determination.

  DOI：

  10.1021/ja973272j

文献信息

• Carbonyl Complexes of Iron(II), Ruthenium(II), and Osmium(II) 5,10,15,20-Tetraphenylporphyrinates:  A Comparative Investigation by X-ray Crystallography, Solid-State NMR Spectroscopy, and Density Functional Theory
  作者：Renzo Salzmann、Christopher J. Ziegler、Nathalie Godbout、Michael T. McMahon、Kenneth S. Suslick、Eric Oldfield

  DOI：10.1021/ja9740069

  日期：1998.11.1

  characterized via single-crystal X-ray diffraction methods iron(II), ruthenium(II), and osmium(II) carbonyl derivatives of (1-methylimidazole)(5,10,15,20-tetraphenylporphyrinate) [(5,10,15,20-tetraphenylporphyrinate = TPP)], Fe(TPP)(CO)(1-MeIm)·toluene, Ru(TPP)(CO)(1-MeIm)·chloroform, and Os(TPP)(CO)(1-MeIm)·chloroform, together with the osmium(II) pyridine adduct Os(TPP)(CO)(py)·2benzene. The crystallographic

  我们已经通过单晶 X 射线衍射方法合成并表征了（1-甲基咪唑）（5,10,15,20-四苯基卟啉）的铁（II）、钌（II）和锇（II）羰基衍生物[（ 5,10,15,20-四苯基卟啉酸盐 = TPP)]、Fe(TPP)(CO)(1-MeIm)·甲苯、Ru(TPP)(CO)(1-MeIm)·氯仿和 Os(TPP)( CO)(1-MeIm)·氯仿，以及锇(II)吡啶加合物Os(TPP)(CO)(py)·2苯。晶体学结果允许对可由 TPP、Fe、Ru、Os 和两种轴向碱基 1-甲基咪唑和吡啶制备的所有六种羰基金属卟啉进行详细的结构比较。所有三种 (Fe, Ru, Os) 1-甲基咪唑配合物的结构都显示出主要的鞍形畸变，畸变程度为 Fe > Ru ∼ Os。对于吡啶配合物，卟啉环平面度的偏差比 1-甲基咪唑物种的偏差小一个数量级。所有配合物中的 M-C-O 键角都在 176.8-17...
• Differential Sensing of Protein Influences by NO and CO Vibrations in Heme Adducts
  作者：Mohammed Ibrahim、Changliang Xu、Thomas G. Spiro

  DOI：10.1021/ja064859d

  日期：2006.12.1

  Heme proteins bind the gaseous ligands XO (X = C, N, O) via backbonding from Fe d(pi) electrons. Backbonding is modulated by distal interactions of the bound ligand with the surrounding protein and by variations in the strength of the trans proximal ligand. Vibrational modes associated with FeX and XO bond stretching coordinates report on these interactions, but the interpretive framework developed for CO adducts, involving anticorrelations of nu FeC and nu CO, has seemed not to apply to NO adducts. We have now obtained an excellent anticorrelation of nu FeN and nu NO, via resonance Raman spectroscopy on (N-methylimidazole)Fe(II)TPP-Y(NO), where TPP-Y is tetraphenylporphine with electron-donating or -withdrawing substituents, Y, that modulate the backbonding; the problem of laser-induced dissociation of the axial base was circumvented by using frozen solutions. New data are also reported for CO adducts. The anticorrelations are supported by DFT calculations of structures and spectra. When protein data are examined, the NO adducts show large deviations from the modeled anticorrelation when there are distal H-bonds or positive charges. These deviations are proposed to result from closing of the FeNO angle due to a shift in the valence isomer equilibrium toward the Fe(III)(NO-) form, an effect that is absent in CO adducts. The differing vibrational patterns of CO and NO adducts provide complementary information with respect to protein interactions, which may help to elucidate the mechanisms of ligand discrimination and signaling in heme sensor proteins.