推荐产品
等级
Sigma Grade
mp
173-177 °C (lit.)
ε (消光系数)
>12,000 at 510 nm in 0.1 M NaOH at 1 M
>7,000 at 385 nm at 1 M
SMILES字符串
Oc1ccc(cc1O)[N+]([O-])=O
InChI
1S/C6H5NO4/c8-5-2-1-4(7(10)11)3-6(5)9/h1-3,8-9H
InChI key
XJNPNXSISMKQEX-UHFFFAOYSA-N
基因信息
rat ... Nos1(24598)
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应用
分光光度法标准品
替代产品
产品编号
说明
价格
储存分类代码
13 - Non Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
dust mask type N95 (US), Eyeshields, Gloves
法规信息
新产品
Stephanie L Groce et al.
Biochemistry, 44(19), 7175-7188 (2005-05-11)
Homoprotocatechuate 2,3-dioxygenase (WT 2,3-HPCD) isolated from Brevibacterium fuscum utilizes an active site Fe(II) and O(2) to catalyze proximal extradiol cleavage of the aromatic ring of the substrate (HPCA). Here, the conserved active site residue His200 is changed to Gln, Glu
Joseph P Emerson et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 10(7), 751-760 (2005-10-12)
The manganese-dependent 3,4-dihydroxyphenylacetate 2,3-dioxygenase (MndD) from Arthrobacter globiformis CM-2 is an extradiol-cleaving catechol dioxygenase that catalyzes aromatic ring cleavage of 3,4-dihydroxyphenylacetate (DHPA). Based on the recent crystal structure of the MndD-DHPA complex, a series of site-directed mutations were made at
A Chauhan et al.
Journal of applied microbiology, 88(5), 764-772 (2000-05-03)
Pseudomonas cepacia RKJ200 (now described as Burkholderia cepacia) has been shown to utilize p-nitrophenol (PNP) as sole carbon and energy source. The present work demonstrates that RKJ200 utilizes 4-nitrocatechol (NC) as the sole source of carbon, nitrogen and energy, and
Ayelet Fishman et al.
Biotechnology and bioengineering, 87(6), 779-790 (2004-08-27)
After discovering that toluene 4-monooxygenase (T4MO) of Pseudomonas mendocina KR1 oxidizes nitrobenzene to 4-nitrocatechol, albeit at a very low rate, this reaction was improved using directed evolution and saturation mutagenesis. Screening 550 colonies from a random mutagenesis library generated by
Mark F Reynolds et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 8(3), 263-272 (2003-02-18)
Mn(II)-dependent 3,4-dihydroxyphenylacetate 2,3-dioxygenase (MndD) is an extradiol-cleaving catechol dioxygenase from Arthrobacter globiformis that has 82% sequence identity to and cleaves the same substrate (3,4-dihydroxyphenylacetic acid) as Fe(II)-dependent 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD) from Brevibacterium fuscum. We have observed that MndD binds the
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