18010
4-Bromophenol
purum, ≥98.0% (HPLC)
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About This Item
Linear Formula:
BrC6H4OH
CAS Number:
Molecular Weight:
173.01
EC Number:
203-394-4
UNSPSC Code:
12352100
PubChem Substance ID:
Beilstein/REAXYS Number:
1680024
MDL number:
grade
purum
assay
≥98.0% (HPLC)
bp
235-236 °C (lit.)
mp
61-64 °C (lit.), 61-65 °C
SMILES string
Oc1ccc(Br)cc1
InChI
1S/C6H5BrO/c7-5-1-3-6(8)4-2-5/h1-4,8H
InChI key
GZFGOTFRPZRKDS-UHFFFAOYSA-N
signalword
Warning
hcodes
Hazard Classifications
Acute Tox. 4 Oral - Skin Irrit. 2
Storage Class
11 - Combustible Solids
wgk
WGK 2
ppe
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Michael F Davis et al.
Biochemistry, 49(6), 1199-1206 (2010-01-14)
Dehaloperoxidase-hemoglobin (DHP A) is a dual function protein found in the terrebellid polychaete Amphitrite ornata. A. ornata is an annelid, which inhabits estuary mudflats with other polychaetes that secrete a range of toxic brominated phenols. DHP A is capable of
A Meizler et al.
Water science and technology : a journal of the International Association on Water Pollution Research, 62(9), 2016-2020 (2010-11-04)
Horseradish peroxidase (HRP) can be used for the treatment of halogenated phenolic substances. In the presence of hydrogen peroxide phenols are oxidized to form polymers which undergo partial dehalogenation. However, when immobilized, the peroxidase is subject to inactivation due to
Matthew H Sazinsky et al.
The Journal of biological chemistry, 279(29), 30600-30610 (2004-04-21)
The four-component toluene/o-xylene monooxygenase (ToMO) from Pseudomonas stutzeri OX1 is capable of oxidizing arenes, alkenes, and haloalkanes at a carboxylate-bridged diiron center similar to that of soluble methane monooxygenase (sMMO). The remarkable variety of substrates accommodated by ToMO invites applications
Ashlee Plummer et al.
Biochemistry, 52(13), 2218-2227 (2013-03-14)
Dehaloperoxidase (DHP A), a unique multifunctional enzyme, from the marine annelid Amphitrite ornata dehalogenates 2,4,6-tribromophenol to form 2,6-dibromo-1,4-benzoquinone. The catalytic cycle of DHP is similar to that of horseradish peroxidase (HRP), involving a high-valent ferryl heme and two single-electron transfers
Stefan Franzen et al.
Biochimica et biophysica acta, 1824(4), 578-588 (2012-01-18)
The dual functions of the dehaloperoxidase-hemoglobin of Amphitrite ornata leads to a paradox. Peroxidase and hemoglobin functions require ferric and ferrous resting states, respectively. Assuming that hemoglobin function is the dominant function, the starting point for peroxidase activation would be
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