2-(4-hydroxy-phenyl)-cyclopent-1-enecarboxylic acid ethyl ester | 1192170-63-0

• 英文名称: 2-(4-hydroxy-phenyl)-cyclopent-1-enecarboxylic acid ethyl ester
• CAS: 1192170-63-0
• 化学式: C₁₄H₁₆O₃
• 分子量: 232.279
• InChiKey: DVXTXTOJEGHKGM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.89
• 重原子数：
  17.0
• 可旋转键数：
  3.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.36
• 拓扑面积：
  46.53
• 氢给体数：
  1.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  2-(4-hydroxy-phenyl)-cyclopent-1-enecarboxylic acid ethyl ester 在 Tesser's base 作用下， 反应 5.0h， 以90%的产率得到2-(4-hydroxy-phenyl)-cyclopent-1-enecarboxylic acid
  参考文献：
  名称：

  Locked Chromophore Analogs Reveal That Photoactive Yellow Protein Regulates Biofilm Formation in the Deep Sea Bacterium Idiomarina loihiensis

  摘要：

  Idiomarina loihiensis is a heterotrophic deep sea bacterium with no known photobiology. We show that light suppresses biofilm formation in this organism. The genome of I. loihiensis encodes a single photoreceptor protein: a homologue of photoactive yellow protein (PYP), a blue light receptor with photochemistry based on trans to cis isomerization of its p-coumaric acid (pCA) chromophore. The addition of trans-locked pCA to I. loihiensis increases biofilm formation, whereas cis-locked pCA decreases it. This demonstrates that the PYP homologue regulates biofilm formation in I. loihiensis, revealing an unexpected functional versatility in the PYP family of photoreceptors. These results imply that I. loihiensis thrives not only in the deep sea but also near the water surface and provide an example of genome-based discovery of photophysiological responses. The use of locked pCA analogs is a novel and generally applicable pharmacochemical tool to study the in vivo role of PYPs irrespective of genetic accessibility. Heterologously produced PYP from I. loihiensis (II PYP) absorbs maximally at 446 nm and has a pCA pK(a) of 3.4. Photoexcitation triggers the formation of a pB signaling state that decays with a time constant of 0.3 s. FTIR difference signals at 1726 and 1497 cm(-1) reveal that active-site proton transfer during the photocycle is conserved in II PYP. It has been proposed that a correlation exists between the lifetime of a photoreceptor signaling state and the time scale of the biological response that it regulates. The data presented here provide an example of a protein with a rapid photocycle that regulates a slow biological response.

  DOI：

  10.1021/ja9057103
• 作为产物：
  描述：

  2-[4-(tert-butyl-dimethyl-silanyloxy)-phenyl]-cyclopent-1-enecarboxylic acid ethyl ester 在 四丁基氟化铵 作用下， 以 四氢呋喃 为溶剂， 以95%的产率得到2-(4-hydroxy-phenyl)-cyclopent-1-enecarboxylic acid ethyl ester
  参考文献：
  名称：

  Locked Chromophore Analogs Reveal That Photoactive Yellow Protein Regulates Biofilm Formation in the Deep Sea Bacterium Idiomarina loihiensis

  摘要：

  Idiomarina loihiensis is a heterotrophic deep sea bacterium with no known photobiology. We show that light suppresses biofilm formation in this organism. The genome of I. loihiensis encodes a single photoreceptor protein: a homologue of photoactive yellow protein (PYP), a blue light receptor with photochemistry based on trans to cis isomerization of its p-coumaric acid (pCA) chromophore. The addition of trans-locked pCA to I. loihiensis increases biofilm formation, whereas cis-locked pCA decreases it. This demonstrates that the PYP homologue regulates biofilm formation in I. loihiensis, revealing an unexpected functional versatility in the PYP family of photoreceptors. These results imply that I. loihiensis thrives not only in the deep sea but also near the water surface and provide an example of genome-based discovery of photophysiological responses. The use of locked pCA analogs is a novel and generally applicable pharmacochemical tool to study the in vivo role of PYPs irrespective of genetic accessibility. Heterologously produced PYP from I. loihiensis (II PYP) absorbs maximally at 446 nm and has a pCA pK(a) of 3.4. Photoexcitation triggers the formation of a pB signaling state that decays with a time constant of 0.3 s. FTIR difference signals at 1726 and 1497 cm(-1) reveal that active-site proton transfer during the photocycle is conserved in II PYP. It has been proposed that a correlation exists between the lifetime of a photoreceptor signaling state and the time scale of the biological response that it regulates. The data presented here provide an example of a protein with a rapid photocycle that regulates a slow biological response.

  DOI：

  10.1021/ja9057103