160954
对硝基苯磺酸甲酯
99%
别名:
Methyl nosylate, Methyl p-nitrobenzenesulfonate, Methyl p-nitrotosylate
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关于此项目
线性分子式:
O2NC6H4SO3CH3
化学文摘社编号:
分子量:
217.20
UNSPSC Code:
12352100
NACRES:
NA.22
PubChem Substance ID:
EC Number:
228-282-2
Beilstein/REAXYS Number:
2277327
MDL number:
Assay:
99%
Form:
solid
InChI key
RMNJNEUWTBBZPT-UHFFFAOYSA-N
InChI
1S/C7H7NO5S/c1-13-14(11,12)7-4-2-6(3-5-7)8(9)10/h2-5H,1H3
SMILES string
COS(=O)(=O)c1ccc(cc1)[N+]([O-])=O
assay
99%
form
solid
Quality Level
mp
89-92 °C (lit.)
solubility
acetone: soluble 5%, clear, faintly yellow to greenish-yellow
functional group
nitro, sulfonic acid
General description
Reaction between methyl 4-nitrobenzenesulfonate and bromide ions has been studied in mixed single-chain-gemini micellar solutions. Kinetics of SN2 reactions of methyl 4-nitrobenzenesulfonate with ammonia, primary amines, secondary amines, tertiary amines and anionic nucleophiles has been studied.
A Lewendon et al.
The Biochemical journal, 290 ( Pt 1), 15-19 (1993-02-15)
A catalytically essential histidine residue (His-195) of chloramphenicol acetyltransferase (CAT) acts as a general base in catalysis, abstracting a proton from the primary hydroxy group of chloramphenicol. The pKa of His-195 has been determined from the pH-dependence of chemical modification.
O Paquatte et al.
Photochemistry and photobiology, 50(6), 817-825 (1989-12-01)
Vibrio harveyi luciferase, an alpha beta dimer, was effectively inactivated by treatment with the methylation agent methyl p-nitrobenzene sulfonate. However, inactivation of luciferase in the presence of excess amounts of this reagent did not follow pseudo-first-order kinetics. After taking the
S Ishii et al.
Protein science : a publication of the Protein Society, 7(8), 1802-1810 (1999-03-19)
Aromatic L-amino acid decarboxylase (AADC) catalytic mechanism has been proposed to proceed through two consecutive intermediates (i.e., Michaelis complex and the external aldimine). Limited proteolysis of AADC that preferentially digested at the C-terminal side of Arg334 was slightly retarded in
R P Swenson et al.
The Journal of biological chemistry, 259(9), 5585-5590 (1984-05-10)
Incubation of D-amino acid oxidase with excess methyl-p-nitrobenzenesulfonate results in a pseudo-first order, irreversible loss of 95% of the assayable activity using D-phenylglycine as substrate. The rate of inactivation reaches a limiting value of 0.021 min-1 (pH 7.7, 22 degrees
M A Porter et al.
The Journal of biological chemistry, 263(29), 14846-14849 (1988-10-15)
The activity of the Calvin cycle enzyme phosphoribulokinase is coupled to photosynthetic electron transport by reversible oxidation/reduction mediated by thioredoxin-f. Previous studies have shown that one of the regulatory sulfhydryl groups, that of Cys-16, is positioned at the nucleotide-binding domain
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