Fe(II)(octaethylporphyrin)(2-methylimidazole) | 64685-92-3

• 分子结构分类: 有机化合物 - 有机杂环化合物
• 英文名称: Fe(II)(octaethylporphyrin)(2-methylimidazole)
• 英文别名: iron(II) octaethyl porphirin (2-methyl imidazole)；[Fe(OEP)(2-MeHIm)]；[Fe(octaethylporphyrinato)(2-methylimidazole)]
• CAS: 64685-92-3
• 化学式: C₄₀H₅₀FeN₆
• 分子量: 670.724
• InChiKey: MHMRWLYUAQQTBW-YAJYDHHFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  10.0
• 重原子数：
  47.0
• 可旋转键数：
  8.0
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  82.66
• 氢给体数：
  1.0
• 氢受体数：
  3.0

反应信息

• 作为产物：
  描述：

  以 二氯甲烷 为溶剂， 生成 Fe(II)(octaethylporphyrin)(2-methylimidazole)
  参考文献：
  名称：

  Time-resolved resonance Raman investigation of the photoreduction of iron octaethylporphyrin complexes by using the quasi-simultaneous pump/probe measurement technique

  摘要：

  A new technique for general pump/probe resonance Raman measurements was developed and applied successfully to identify a transient species involved in the photoreduction of a ferric porphyrin complex. This technique emphasizes quasi-simultaneous measurements of the pump/probe, pump-only, probe-only, and dark spectra. It is demonstrated that the present method not only brings about a higher signal-to-noise ratio but also provides the correct spectra of intermediates even if slight photodecomposition by pump light illumination is involved. With this device, the time-resolved resonance Raman spectra were observed for a 2-methylimidazole (2MeIm) and methanol (MeOH) complex of (octaethylporphyrinato)iron(III) [Fe(III)(OEP)(2MeIm)(MeOH)] and its meso-deuterated and N-15(4) isotopomers in the time range from 0 ns to 1 mus following photolysis. The transient spectra were probed by the 416-nm pulse (width = 7 ns) after the photoreduction was initiated by a pump pulse at 355 nm. The transient spectrum for the delay time (DELTAt(d)) of 20 ns contained the contribution from the tetracoordinate ferrous intermediate-spin species besides that from the pentacoordinate ferrous high-spin species. The latter dominated the spectrum for DELTAt(d) = 1 mus but was also discernible in the spectrum for DELTAt(d) = 0 ns. Dependences of the spectra on the concentrations of 2MeIm and MeOH were examined for DELTAt(d) = 0 and 100 ns, suggesting the presence of two pathways for the present photoreduction. A plausible mechanism is discussed on the basis of the observed spectra.

  DOI：

  10.1021/j100205a020

文献信息

• Resonance Raman characterization of iron-chlorin complexes in various spin, oxidation, and ligation states. 1. Comparative study with corresponding iron-porphyrin complexes
  作者：Y. Ozaki、K. Iriyama、H. Ogoshi、T. Ochiai、T. Kitagawa

  DOI：10.1021/j100281a011

  日期：1986.11
• State Preparation and Excited Electronic and Vibrational Behavior in Hemes
  作者：J. Reddy Challa、Tissa C. Gunaratne、M. Cather Simpson

  DOI：10.1021/jp063543p

  日期：2006.10.1

  The temporally overlapping, ultrafast electronic and vibrational dynamics of a model five-coordinate, highspin heme in a nominally isotropic solvent environment has been studied for the first time with three complementary ultrafast techniques: transient absorption, time-resolved resonance Raman Stokes, and time-resolved resonance Raman anti-Stokes spectroscopies. Vibrational dynamics associated with an evolving ground-state species dominate the observations. Excitation into the blue side of the Soret band led to very rapid S-2 -> S-1 decay (sub-100 fs), followed by somewhat slower (800 fs) S-1 -> S-0* nonradiative decay. The initial vibrationally excited, non-Boltzmann S-0* state was modeled as shifted to lower energy by 300 cm(-1) and broadened by 20%. On a similar to 10 ps time scale, the S-0* state evolved into its room-temperature, thermal distribution S-0 profile largely through VER. Anti-Stokes signals disappear very rapidly, indicating that the vibrational energy redistributes internally in about 1-3 ps from the initial accepting modes associated with S-1 -> S-0 internal conversion to the rest of the macrocycle. Comparisons of anti-Stokes mode intensities and lifetimes from TRARRS studies in which the initial excited state was prepared by ligand photolysis [Mizutani, T.; Kitagawa, T. Science 1997, 278, 443, and Chem. Rec. 2001, 1, 258] suggest that, while transient absorption studies appear to be relatively insensitive to initial preparation of the electronic excited state, the subsequent vibrational dynamics are not. Direct, time-resolved evaluation of vibrational lifetimes provides insight into fast internal conversion in hemes and the pathways of subsequent vibrational energy flow in the ground state. The overall similarity of the model heme electronic dynamics to those of biological systems may be a sign that the protein's influence upon the dynamics of the heme active site is rather subtle.