2'-<14C>acetonitrile | 7183-57-5

• 分子结构分类: 有机化合物
• 英文名称: 2'-<14C>acetonitrile
• 英文别名: acetonitrile
• CAS: 7183-57-5
• 化学式: C₂H₃N
• 分子量: 43.0415
• InChiKey: WEVYAHXRMPXWCK-NJFSPNSNSA-N

物化性质

• 沸点：
  76-100 °C
• 闪点：
  2 °C

计算性质

• 辛醇/水分配系数(LogP)：
  0
• 重原子数：
  3
• 可旋转键数：
  0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  23.8
• 氢给体数：
  0
• 氢受体数：
  1

安全信息

• 安全说明：
  S16,S26,S36/37/39,S45
• 危险类别码：
  R23/24/25,R36/37/38,R11
• 危险品运输编号：
  UN 1648 3/PG 2

反应信息

• 作为反应物：
  描述：

  sodium hydroxide 、 2'-<14C>acetonitrile 以 水 为溶剂， 生成 [14C]-乙酸
  参考文献：
  名称：

  Gmelin Handbuch der Anorganischen Chemie, Gmelin Handbook: C: MVol.C4, 6.1.5, page 125 - 127

  摘要：

  DOI：
• 作为产物：
  描述：

  potassium cyanide 、 methyl hydrogensulfate 以 not given 为溶剂， 生成 2'-<14C>acetonitrile
  参考文献：
  名称：

  Martin Municio, A., Anales de la Real Sociedad Espanola de Fisica y Quimica, Serie B: Quimica, 1955, vol. 51, p. 469 - 476

  摘要：

  DOI：

文献信息

• Mechanistic Studies of the Inactivation of Inducible Nitric Oxide Synthase by <i>N</i>⁵-(1-Iminoethyl)-<scp>l</scp>-ornithine (<scp>l</scp>-NIO)
  作者：Walter Fast、Dejan Nikolic、Richard B. Van Breemen、Richard B. Silverman

  DOI：10.1021/ja982318l

  日期：1999.2.1

  Nitric oxide synthase (NOS) catalyzes the conversion of L-arginine to L-citrulline and nitric oxide. N-5-(1-Iminoethyl)-L-ornithine (L-NIO, 5) is a natural product known to inactivate NOS, but the mechanism of inactivation is unknown. Upon incubation of iNOS with L-NIO a type I binding difference spectrum is observed, indicating that binding at the substrate binding site occurs. L-NIO is shown to be a time-dependent, concentration-dependent, and NADPH-dependent irreversible inhibitor of iNOS with K-I and k(inact) values of 13.7 +/- 1.6 mu M and 0.073 +/- 0.003 min(-1), respectively. During inactivation the heme chromophore is partially lost (Figure 1); HPLC shows that the loss corresponds to about 50% of the heme. Inclusion of catalase during incubation does not prevent heme loss. N-5-(1-Imino-2-[C-14]ethyl)-L-ornithine (11) inactivates iNOS, but upon dialysis or gel filtration, no radioactivity remains bound to the protein or to a cofactor. The only radioactive product detected after enzyme inactivation is Nw-hydroxy-L-NIO (12); no C-omega-hydroxy-L-NIO (13) or N-delta-acetyl-L-ornithine (14) is observed (Figure 2). The amount of 12 produced during the inactivation process is 7.7 +/- 0.2 equiv per inactivation event. Incubations of 12 with iNOS show time-, concentration-, and NADPH-dependent inactivation that is not reversible upon dilution into the assay solution. Incubations that include an excess of L-arginine or with substitution of NADP(+) for NADPH result in no significant loss of enzyme activity. The K-I and k(inact) values for 12 an 830 +/- 160 mu M and 0.0073 +/- 0.0007 min(-1), respectively. The magnitude of these kinetic constants (compared with those of 5) suggest that 12 is not an intermediate of L-NIO inactivation of iNOS. Compound 12 also is a substrate for iNOS, exhibiting saturation kinetics with K-m and k(cat) values of 800 +/- 85 mu M and 2.22 min(-1), respectively; the product is shown to be N-delta-acetyl-L-ornithine (14) (Figure 3). The k(cat) and k(inact) values for 12 can be compared directly to give a partition ratio (k(cat)/k(inact)) for inactivation of 304; i.e., there are 304 turnovers to give NO per inactivation event. This high partition ratio further supports the notion that 12 is not involved in L-NIO inactivation of iNOS. C-omega-Hydroxy-L-NIO (13) is not an inactivator of iNOS. These results suggest that L-NIO inactivation occurs after an oxidation step (NADPH is required for inactivation) but prior to a hydroxylation step (12 and 13 are not involved). Inactivation of iNOS by N-5-(1-imino-2-[H-2(3)]-ethyl)-L-ornithine (15) exhibits a kinetic isotope effect on (H)k(inact)/(D)k(inact) of 1.35 +/- 0.08 and on H(k(inact)/K-I)/(D)(k(inact)/K-I) of 1.51 +/- 0.3, suggesting that the methyl C-H bond is cleaved in a partially rate-determining step prior to hydroxylation, and that leads to inactivation.A new NADPH-dependent 400 nm peak in the HPLC of L-NIO-inactivated iNOS is produced (Figure 4). LC-electrospray mass spectrometry (Figure 5) demonstrates the mit of the new metabolite to be 583, which is shown to correspond to biliverdin (23) (Figures 6 and 7). Two possible mechanisms for the formation of biliverdin during inactivation are proposed (Schemes 10 and 11). When 14 is incubated with iNOS, time-, concentration-, and NADPH-dependent loss of enzyme activity is observed (K-I and k(inact) values are 490 mM and 0.24 min(-1), respectively); iNOS inactivation by 14 can be prevented by inclusion of L-arginine, but not D-arginine, in the inactivation mixtures, suggesting that the inactivator acts at the arginine binding site. However, 14 is not produced from L-NIO (Figure 2) and, therefore, is not involved in L-NIO inactivation.
• Taugbol, K., Chemical Abstracts, JENER Rept. Nr. 29 (1954), S. 1/11, 1956, p. 168
  作者：Taugbol, K.

  DOI：——

  日期：——