1-Methoxynaphthalene
(Synonyms: 1-萘甲醚) 目录号 : GC61715
1-Methoxynaphthalene 用于研究细胞色素 c 过氧化物酶的过氧化酶活性。它用作合成异戊二烯基萘酚的前体，具有抗氧化活性
Cas No.:2216-69-5
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
1-Methoxynaphthalene is used as the substrate to investigate the activity of cytochrome c peroxidase (CcP). 1-Methoxynaphthalene also can be used to synthesize prenyl naphthalen-ols[1][2].
[1]. Erman JE, et, al. Peroxygenase activity of cytochrome c peroxidase and three apolar distal heme pocket mutants: hydroxylation of 1-methoxynaphthalene. BMC Biochem. 2013 Jul 30;14:19. [2]. Shindo K, et, al. Production of novel antioxidative prenyl naphthalen-ols by combinational bioconversion with dioxygenase PhnA1A2A3A4 and prenyltransferase NphB or SCO7190. Biosci Biotechnol Biochem. 2011;75(3):505-10.
| Cas No. | 2216-69-5 | SDF | |
| 别名 | 1-萘甲醚 | ||
| Canonical SMILES | COC1=C2C=CC=CC2=CC=C1 | ||
| 分子式 | C11H10O | 分子量 | 158.2 |
| 溶解度 | 储存条件 | Store at -20°C | |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 6.3211 mL | 31.6056 mL | 63.2111 mL |
| 5 mM | 1.2642 mL | 6.3211 mL | 12.6422 mL |
| 10 mM | 0.6321 mL | 3.1606 mL | 6.3211 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Photolysis of ((3-(Trimethylsilyl)propoxy)phenyl)phenyliodonium salts in the presence of 1-naphthol and 1-Methoxynaphthalene
J Org Chem 2000 Jun 2;65(11):3484-8.PMID:10843635DOI:10.1021/jo000058w.
Direct photolysis of ((3-trimethylsilylpropoxy)phenyl)phenyliodonium salts with different counteranions (Cl(-), SbF(6)(-), and B(C(6)F(5))(4)(-)) in methanol leads to products by both heterolytic and homolytic processes. In the presence of 1-naphthol and 1-Methoxynaphthalene, products formed by a heterolytic reaction disappear, suggesting an electron-transfer process occurs between excited 1-naphthol/1-Methoxynaphthalene and the iodonium salts. In the case of 1-Methoxynaphthalene, three phenylated methoxynaphthalene isomers are produced. These are produced as radical coupling products from the phenyl radical and 1-Methoxynaphthalene radical cation.
Peroxygenase activity of cytochrome c peroxidase and three apolar distal heme pocket mutants: hydroxylation of 1-Methoxynaphthalene
BMC Biochem 2013 Jul 30;14:19.PMID:23895311DOI:10.1186/1471-2091-14-19.
Background: The cytochrome P450s are monooxygenases that insert oxygen functionalities into a wide variety of organic substrates with high selectivity. There is interest in developing efficient catalysts based on the "peroxide shunt" pathway in the cytochrome P450s, which uses H2O2 in place of O2/NADPH as the oxygenation agent. We report on our initial studies using cytochrome c peroxidase (CcP) as a platform to develop specific "peroxygenation" catalysts. Results: The peroxygenase activity of CcP was investigated using 1-Methoxynaphthalene as substrate. 1-Methoxynaphthalene hydroxylation was monitored using Russig's blue formation at standard reaction conditions of 0.50 mM 1-Methoxynaphthalene, 1.00 mM H2O2, pH 7.0, 25°C. Wild-type CcP catalyzes the hydroxylation of 1-Methoxynaphthalene with a turnover number of 0.0044 ± 0.0001 min-1. Three apolar distal heme pocket mutants of CcP were designed to enhance binding of 1-Methoxynaphthalene near the heme, constructed, and tested for hydroxylation activity. The highest activity was observed for CcP(triAla), a triple mutant with Arg48, Trp51, and His52 simultaneously mutated to alanine residues. The turnover number of CcP(triAla) is 0.150 ± 0.008 min-1, 34-fold greater than wild-type CcP and comparable to the naphthalene hydroxylation activity of rat liver microsomal cytochrome P450. While wild-type CcP is very stable to oxidative degradation by excess hydrogen peroxide, CcP(triAla) is inactivated within four cycles of the peroxygenase reaction. Conclusions: Protein engineering of CcP can increase the rate of peroxygenation of apolar substrates but the initial constructs are more susceptible to oxidative degradation than wild-type enzyme. Further developments will require constructs with increased rates and selectivity while maintaining the stability of wild-type CcP toward oxidative degradation by hydrogen peroxide.
Experimental (FT-IR and FT-Raman), electronic structure and DFT studies on 1-Methoxynaphthalene
Spectrochim Acta A Mol Biomol Spectrosc 2011 Aug;79(3):646-53.PMID:21530378DOI:10.1016/j.saa.2011.03.051.
In this work, FT-IR and FT-Raman spectra of 1-methoxynapthalene (C(11)H(10)O) have been reported in the regions 4000-400 cm(-1) and 3500-100 cm(-1), respectively. Density functional method (DFT) has been used to calculate the optimized geometrical parameters, atomic charges, vibrational wavenumbers and intensity of the vibrational bands. The vibrational frequencies have been calculated and scaled values are compared with experimental FT-IR and FT-Raman spectra. The structure optimizations and normal coordinate force field calculations are based on density functional theory (DFT) method with B3LYP/3-21G, B3LYP/6-31G, B3LYP/6-31G(d,p) and B3LYP/6-311++G(d,p) basis sets. The complete vibrational assignments of wavenumbers are made on the basis of potential energy distribution (PED). The optimized geometric parameters are compared with experimental values of naphthoic acid. The results of the calculation shows excellent agreement between experimental and calculated frequencies in B3LYP/6-311++G(d,p) basis set. The effects due to the substitutions of methyl group and carbon-oxygen bond are also investigated. A study on the electronic properties, such as excitation energies and wavelengths, were performed by time-dependent DFT (TD-DFT) approach. HOMO and LUMO energies are calculated that these energies show charge transfer occurs within the molecule.
NMR and calculational studies on the regioselective lithiation of 1-Methoxynaphthalene
J Am Chem Soc 2002 Jul 24;124(29):8699-706.PMID:12121114DOI:10.1021/ja010456w.
1-Methoxynaphthalene (1) undergoes regioselective lithiation in position 2 (n-BuLi/TMEDA) or in position 8 (t-BuLi), respectively. The detected formation of a n-BuLi/1 complex (1:1 n-BuLi/1 mixture) appears to have only minor influence on the regioselectivity (both products are obtained). The exchange of hydrogen atom H2 by deuterium results in a remarkably reduced reaction rate for the lithiation with n-BuLi in THF-d(8). This isotope effect and the formation of the thermodynamically less favorable 2-lithio compound suggest a kinetically controlled mechanism. The lack of an isotope effect for the reaction of 8-deuterio-1-methoxynaphthalene with t-BuLi and the formation of the thermodynamically preferred 8-lithiated product indicate a thermodynamically controlled mechanism. Slow conversion of the 2- into the 8-lithiated species (at higher temperatures) gives further evidence that n-BuLi and t-BuLi afford the kinetically and thermodynamically preferred products, respectively.
Biotransformation of phenanthrene and 1-Methoxynaphthalene with Streptomyces lividans cells expressing a marine bacterial phenanthrene dioxygenase gene cluster
Biosci Biotechnol Biochem 2001 Aug;65(8):1774-81.PMID:11577717DOI:10.1271/bbb.65.1774.
The phdABCD gene cluster in a marine bacterium Nocardioides sp. strain KP7 codes for the multicomponent enzyme phenanthrene dioxygenase. phdA encoding an iron-sulfur protein large subunit alpha, phdB encoding its small subunit beta, phdC encoding ferredoxin, and phdD encoding ferredoxin reductase, were replaced in such a way that the termination codons of the preceding open reading frames were overlapped with the initiation codons of the following genes. This manipulated phdABCD gene cluster was positioned downstream of the thiostrepton-inducible promoter PtipA in a high-copy-number vector pIJ6021, and introduced into the gram-positive, soil-inhabiting, filamentous bacterium Streptomyces lividans. The recombinant S. lividans cells converted phenanthrene into a cis-diol form, which was determined to be cis-3,4-dihydroxy-3,4-dihydrophenanthrene by its UV spectral data as well as HPLC property, using the authentic sample for comparison. This biotransformation proceeded very efficiently; 200 microM and 2 mm of phenanthrene were almost completely converted to its cis-diol form in 6 h and 32 h, respectively. In addition, the S. lividans cells carrying the phdABCD gene cluster were found to transform 1-Methoxynaphthalene to two products, which were identified to be 8-methoxy-2-naphthol in addition to 8-methoxy-1,2-dihydro-1,2-naphthalenediol by their EI-MS, 1H- and 13C-NMR spectral data.