6633-40-5Relevant academic research and scientific papers
Cross-conjugation vs. linear conjugation in donor-bridge-acceptor nitrophenol chromophores
Christensen, Mikkel Andreas,Della Pia, Eduardo Antonio,Houmoller, Jorgen,Thomsen, Sean,Wanko, Marius,Bond, Andrew D.,Rubio, Angel,Brondsted Nielsen, Steen,Brondsted Nielsen, Mogens
, p. 2044 - 2052 (2014/04/17)
The influence of cross-conjugation vs. linear conjugation on the electronic communication between donor and acceptor groups in phenol(ate)-bridge- nitrobenzene chromophores was investigated by solution and gas-phase absorption spectroscopy, fluorescence s
Molecular engineering of organic sensitizers with planar bridging units for efficient dye-sensitized solar cells
Lim, Kimin,Ju, Myung Jong,Na, Jongbeom,Choi, Hyeju,Song, Min Young,Kim, Byeonggwan,Song, Kihyung,Yu, Jong-Sung,Kim, Eunkyoung,Ko, Jaejung
, p. 9442 - 9446 (2013/07/26)
Here comes the sun: Three highly efficient organic sensitizers with sterically hindered fluorenyl units and planar indenothiophene derivatives were designed and synthesized (see figure). Devices based on one of these compounds, JK-303, gave overall conversion efficiencies of 8.69, 9.04, 7.27, and 5.82 % using I-/I3-, CoII/CoIII, polymer gel, and solid-state electrolytes, respectively. These efficiencies are some of the highest reported for DSSCs based on organic sensitizers. Copyright
Preneoplastic lesions, DNA adduct formation and mutagenicity of 5-, 7- and 9 -hydroxy-2-nitrofluorene, metabolites of the air pollutant 2-nitrofluorene
Cui, Xian-Shu,Bergman, Jan,Moeller, Lennart
, p. 147 - 155 (2007/10/03)
The metabolites of 2-nitrofluorene (NF), 5-, 7- and 9-OH-2-nitrofluorene (OH-NF) were compared for their genotoxicity. Seventy-two hours after intraperitoneal administration of these substances individually to rats (100 mg/kg body wt.), DNA adducts in liver tissue were analyzed with 32P-TLC and 32P-HPLC. An in vivo liver model was used to test the initiating capacity of the said substances for the formation of preneoplastic lesions. 5-OH-NF showed low capacity to induce DNA adduct formation and low potential as initiator to induce preneoplastic lesions-foci/nodules in the liver of rats. Both 7- and 9-OH-NF induced DNA adducts and preneoplastic liver lesions but with smaller quantities compared to NF. It seems that 7- and 9-OH-NF can not be considered as detoxification products of NF. In general, the initiating capacity of these substances for the formation of preneoplastic lesions has a good correlation with their potency to form DNA adducts.
Mechanism-Based Inactivation of N-Arylhydroxamic Acid N,O-Acyltransferase by 7-Substituted-N-hydroxy-2-acetamidofluorenes
Marhevka, Virginia C.,Ebner, Nancy A.,Sehon, Russell D.,Hanna, Patrick E.
, p. 18 - 24 (2007/10/02)
N-Arylhydroxamic acid N,O-acyltransferase (AHAT) catalyzes the transfer of the N-acetyl group from N-arylhydroxamic acids to arylamines.In the absence of an arylamine acceptor, AHAT catalyzes the conversion of N-arylhydroxamic acids to reactive electrophilic intermediates that become irreversibly bound to cellular nucleophiles, including those present on AHAT itself.As a part of an investigation of the AHAT-catalyzed bioactivation process, a series of 7-substituted analogues of N-hydroxy-2-acetamidofluorene (1) was synthesized and evaluated in vitro as substrates andinactivators of a partially purified hamster hepatic AHAT preparation.All of the compounds functioned as acetyl donors in the AHAT-catalyzed transacetylation of 4-aminoazobenzene (AAB) and all of them were inactivators of AHAT.The inactivation process exhibited apparent first-order kinetics, and the 7-methoxy compound exhibited the largest inactivation rate constant.Quantitative structure-activity analysis provided support for the concept that positively charged species are involved in the inactivation of AHAT by this series of compounds.Results of experiments in which nucleophilic trapping agents such as glutathione, cysteine, methionine, guanosine phosphate, and tRNA were included in incubation mixtures with AHAT and the N-arylhydroxamic acids indicated that electrophiles which diffuse away from the enzyme active site participate in the inactivation process.
