Enhanced reactivity of a flavin bound to quaternized poly(4-vinylpyridine) via 8-position. A model system of a flavin coenzyme covalently-linked to enzymes.
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概要
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The rate constants for the reaction of the title flavin and the monomeric analogues with 1-benzyl-1,4-dihydronicotinamide (BzlNH), 1-nitroethanide ion, glutathione (GSH), and thiophenol (PhSH) were determined at 30 °C. Although the reactivity of 8α-AcHisFl is slightly improved as compared with that of unmodified flavin, the rate constants for 8α-PyFl which is expected to mimic the reactivity of protonated 8α-AcHisFl were significantly increased. The rate constants for the oxidation of anionic reductants(1-nitroethanide ion, GSH, and PhSH) were further increased by immobilization of the 8α-PyFl structure in quaternized 4VP polymers. The kinetic results implicate that (1) with regard to the action of a flavin covalently-linked to enzymes <I>via</I> histidine residue, the flavin must be more reactive in acidic pH region due to protonation of the histidine than in basic pH region, (2) the cationic polyelectrolyte environment accelerates selectively the oxidation of anionic reductants, and (3) the title flavin serves as a strong, selective oxidizing agent under ambient reaction conditions.
- 公益社団法人 日本化学会の論文
著者
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Shinkai Seiji
Department Of Applied Chemistry Faculty Of Engineering Kyushu University
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Mori Kenji
Department Of Agricultural Chemistry College Of Science And Technology The University Of Tokyo
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MANABE Osamu
Department of Applied Chemistry, Faculty of Engineering, Nagasaki University
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Manabe Osamu
Department of Industrial Chemistry, Faculty of Engineering, Nagasaki University
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Kusano Yumiko
Department of Industrial Chemistry, Faculty of Engineering, Nagasaki University
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