• Textile Coloration and Finishing
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• v.4 no.2
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• pp.64-68
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• 1992

The charge-transfer(CT) complexes derived from phenothiazine as donor and quinonoid compounds as accepters were evaluated as coloring matter. Light fastness of the intermolecular charge-transfer(CT) complex dyes as well as absorption wavelength is an important factor when the complexes are applied to coloring matters. The photofading mechanism of CT complex dyes of phenothiazine and accepters were examined. The addition of effective radical scavenger, antioxidant and photostabilizer gave a remarkable enhancement of the photostability of CT dyes.

• Bulletin of the Korean Chemical Society
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• v.9 no.4
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• pp.257-258
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• 1988

• Bulletin of the Korean Chemical Society
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• v.18 no.4
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• pp.374-379
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• 1997

The rate constants for the nucleophilic addition of thiophenol derivatives (p-OCH3, H, p-CH3, m-CH3, p-Br and p-NO2) to 4'-[N-(9-acridinyl)]-1'-(N-methanesulfonyl)-3'-methoxyquinonediimide (AMQD) were determined by ultraviolet spectrophotometer in water at 5 ℃, and rate equations which can be applied over a wide pH range were obtained. On the basis of pH-rate profile, Bronsted plot, adduct analysis, general base catalysis and substituent effect, a plausible mechanism of this addition reaction was proposed: Below pH 2.5, the reaction proceeded by the addition of thiophenol molecule to 6'-position of quinonoid after protonation at the acridinyl nitrogen. Above pH 6.2, the addition of sulfide anion to 6'-position of quinonoid was rate controlling. However, in the range of pH 3.0-6.0, these two reactions occured competively.

• Journal of Microbiology and Biotechnology
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• v.16 no.9
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• pp.1434-1440
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• 2006

The stable anchorage of pyridoxal 5'-phosphate (PLP) in the active site of D-amino acid transaminase (D-AT) is crucial for the enzyme catalysis. The three-dimensional structure of D-AT revealed that Glu32 is one of the active site groups that may playa role in PLP binding. To prove the role of Glu32 in PLP stability, we firstly checked the rate of the potential rate-limiting step. The kinetic analysis showed that the rate of the ${\alpha}$-deprotonation step reduced to 26-folds in E32A mutant enzyme. Spectral analyses of the reaction of D-AT with D-serine revealed that the E32A mutant enzyme failed to stabilize the key enzyme-substrate intermediate, namely a quinonoid intermediate (E-Q). Finally, analysis of circular dichroism (CD) on the wild-type and E32A mutant enzymes showed that the optical activity of PLP in the enzyme active site was lost by the removal of the carboxylic group, proving that Glu32 is indeed involved in the cofactor anchorage. The results suggested that the electrostatic interaction network through the groups from PLP, Glu32, His47, and Arg50, which was observed from the three-dimensional structure of the enzyme, plays a crucial role in the stable anchorage of the cofactor to give necessary torsion to the plane of the cofactor-substrate complex.

• BMB Reports
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• v.35 no.3
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• pp.306-312
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• 2002

The effects of salts on the biochemical properties of D-amino acid aminotransferase from Bacillus sp. YM-1 have been studied to elucidate both the inhibitory effects of salts on the activity and the protective effects of salts on the substrate-induced inactivation. The results from UV-visible spectroscopy studies on the reaction of the enzyme with D-serine revealed that salt significantly reduced the rate of the formation of the quinonoid intermediate and its accumulation. The kinetic and spectroscopy studies of the reaction with $\alpha$-[$^2H$]-DL-serine in different concentrations of NaCl provided evidence that the rate-limiting step was changed from the deprotonation of the external aldimine to another step(s), presumably to the hydrolysis of the ketimine. Gel filtration chromatography data in the presence of NaCl showed that the enzyme volume was reduced sharply with the increasing NaCl concentration, up to 100 mM. An additional increase of the NaCl concentration did not affect the elution volume, which suggests that the enzyme has a limited number of salt-binding groups. These results provide detailed mechanistic evidence for the way salts inhibit the catalytic activity of D-amino acid aminotransferase.

• Archives of Pharmacal Research
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• v.22 no.4
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• pp.384-390
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• 1999

Thirty-four glutathione conjugates of 5,8-dimethoxy-1,4-naphthoquinones (DMNQ) were synthesized and their structure was determined. The yield of GSH conjugate was dependent on size of alkyl group; the longer the size of alkyl group was, the lower was the yield. It was also found that the length of alkyl side chain influenced the chemical shift of quinonoid protons; the quinonoid protons of 2-glutathionyl DMNQ derivatives with R=H to propyl, 6.51-6.59 ppm vs. other ones with R=butyl to heptyl, 6.64-6.68 ppm. this was explained to be due to a folding effect of longer alkyl group. Glutathione (GSH) reacted with DMNQ derivative first to form a 1,4-adduct (2- or 3-glutathionyl-1,4-dihydroxy-5,8-dimethoxynaphthalenes) and then the adduct was autooxidized to 2- or 3-glutathionyl-DMNQ derivatives. Moreover, GSH reduced DMNQ derivatives to their hydrogenated products. It was suggested that such an organic reaction might play an important role for a study of metabolism or toxicity of DMNQ derivative sin the living cells.

• Journal of the Korean Chemical Society
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• v.40 no.12
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• pp.733-740
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• 1996

The rate constants for the hydrolysis of 4'-[N-(9-acridinyl)]-1'-(N-methanesulfonyl)-3'-methoxyquinonediimide(AMQD) were determined by ultraviolet visible spectrophotometer in water at $25^{\circ}C.$ The rate equation which could be applied over wide pH ranges were obtained. On the basis of pH-rate profile, Bronsted plot, hydrolysis product analysis, general base catalysis and substituent effect, the plausible hydrolysis mechanism was proposed: Below pH 3.00, the hydrolysis reaction was proceeded by the attack of water to 4'-position of quinonoid after protonation at nitrogen of acridinyl and between pH 3.00 and 9.00, the addition of water and hydroxide occurred competitively. However, above pH 9.00, the rate constants were dependent upon only the concentration of hydroxide ion.

• BMB Reports
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• v.32 no.4
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• pp.321-325
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• 1999

NAD(P)H-quinone oxidoreductase (EC 1. 6. 99. 2) was purified form S. cerevisiae. The enzyme readily reduced 2,6-dichlorophenolindophenol, a quinonoid redox dye, as well as substituted benzo- and naphthoquinones, and could accept electrons from either NADH or NADPH. The purified NAD(P)H-quinone oxidoreductase turned out to be capable of reducing nitrosoarenes as well as a variety of quinones. A chemical-trapping technique using 4-chloro-1-naphthol was used to show that the N,N-dimethyl-p-benzoquinonediiminium cation was produced in the reduction of 4-nitroso-N,N-dimethylaniline catalyzed by NAD(P)H-quinone oxidoreductase.

• Bulletin of the Korean Chemical Society
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• v.10 no.1
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• pp.57-60
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• 1989

UV irradiation of anthraquinone and diphenylacetylene in benzene gave 1:1 photoadduct (7) and cyclization product (8). The photoreaction of anthrone and diphenylacetylene in dichloromethane afforded the photooxidation products (7, 8, and 9) in air. The photoproduct (7) underwent the cyclization reaction during the purification by the column chromatography (silica gel). When irradiated with 350 nm UV light, the product (11) of benzil reacted with diphenylacetylene to give a photoadduct(12).

• Bulletin of the Korean Chemical Society
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• v.26 no.8
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• pp.1170-1176
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• 2005

The structures and conformations of ortho-, meta-, and para-methyl red (MR) upon proton gain and loss were studied by density functional calculations, and compared to methyl yellow for the effects of a carboxyl substitution. Internal hydrogen bonding causes the geometry of neutral o-MR planar, otherwise twist. Monoprotonated species of MR are planar where the proton is attached to $\beta$-azo nitrogen. This loses its azo character a bit, and shows strong delocalization characterized as a quinonoid canonical structure. Di-protonated species of MR is proved to hold two protons at the amino and $\alpha$-azo nitrogen atoms, and planar. It regains somewhat of its azo character, but still shows fairly delocalized property in terms of carbocationic canonical structures. The carboxyl substitution on 4-dimethylamino-trans-azobenzene structure has some delocalization effects on the geometry or conformation of MR derivatives whether neutral, mono-, di- or de-protonated.