N9608
4′-Nitroacetophenone
98%
Synonym(s):
1-(4-Nitrophenyl)ethan-1-one, 1-(4-Nitrophenyl)ethanone, 1-Acetyl-4-nitrobenzene, 4-Nitrophenyl methyl ketone, 4′-Nitroacetophenone, p-Acetylnitrobenzene
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All Photos(3)
About This Item
Linear Formula:
O2NC6H4COCH3
CAS Number:
Molecular Weight:
165.15
Beilstein:
607777
EC Number:
MDL number:
UNSPSC Code:
12352100
PubChem Substance ID:
NACRES:
NA.22
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Quality Level
Assay
98%
form
crystals
bp
202 °C (lit.)
mp
75-78 °C (lit.)
SMILES string
CC(=O)c1ccc(cc1)[N+]([O-])=O
InChI
1S/C8H7NO3/c1-6(10)7-2-4-8(5-3-7)9(11)12/h2-5H,1H3
InChI key
YQYGPGKTNQNXMH-UHFFFAOYSA-N
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Related Categories
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Biochemical pharmacology, 45(8), 1711-1714 (1993-04-22)
Interindividual variability of carbonyl reductase levels in human livers (N = 11) was examined by measuring reductase activity toward various substrates and by western blot analysis using anti-rat ovarian carbonyl reductase CR2 antibody. The carbonyl reductase activity toward p-nitrobenzaldehyde (PNBA)
A Hissung et al.
International journal of radiation biology and related studies in physics, chemistry, and medicine, 39(1), 63-71 (1981-01-01)
The reactions of the one electron adduct of 2'-deoxyadenosine dA(-), in aqueous solutions have been studied using pulse radiolysis techniques with optical absorption and conductivity detection. The dA(-) radical anion itself shows a weak and featureless optical absorption at greater
J M Wong et al.
Pharmacogenetics, 3(2), 110-115 (1993-04-01)
The enzyme family carbonyl reductase, which catalyses the reduction of xenobiotic as well as endogenous ketones and aldehydes, has not been very well studied in terms of its biological functions and structural aspects. The aim of the present study was
K Tatsumi et al.
Journal of pharmacobio-dynamics, 4(2), 101-108 (1981-02-01)
The electron transfer mechanism in the reduction of aromatic nitro compounds by xanthine oxidase was investigated using methyl p-nitrobenzoate and p-nitroacetophenone as substrates. Methyl p-nitrobenzene was reduced by both one-electron and more than two-electron transfer mechanisms in the enzyme-electron donor
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