TY - JOUR
T1 - A flavoenzyme model
T2 - Facile oxidation of thiols by a flavin immobilized in cationic polyelectrolytes
AU - Shinkai, Seiji
AU - Yamada, Shinji
AU - Ando, Reiko
AU - Kunitake, Toyoki
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1980/6
Y1 - 1980/6
N2 - The reactions of a polymer-bound flavin with thiols (2-mercaptoethanol, glutathione, thiophenol, and 1,4-butanedithiol) are remarkably accelerated, when compared with that of a monomeric flavin. The rate enhancements observed were 30- to 6000-fold. In particular, thiophenol which had been believed not to be oxidized by flavin in nonenzymatic systems was oxidized most rapidly among the monothiols examined. The reaction rates were improved by incorporation of a dodecyl group into the flavin-containing polymer. Therefore, the hydrophobic nature of the cationic polymer matrix was concluded to be responsible for the large rate enhancement among other factors.
AB - The reactions of a polymer-bound flavin with thiols (2-mercaptoethanol, glutathione, thiophenol, and 1,4-butanedithiol) are remarkably accelerated, when compared with that of a monomeric flavin. The rate enhancements observed were 30- to 6000-fold. In particular, thiophenol which had been believed not to be oxidized by flavin in nonenzymatic systems was oxidized most rapidly among the monothiols examined. The reaction rates were improved by incorporation of a dodecyl group into the flavin-containing polymer. Therefore, the hydrophobic nature of the cationic polymer matrix was concluded to be responsible for the large rate enhancement among other factors.
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U2 - 10.1016/0045-2068(80)90024-3
DO - 10.1016/0045-2068(80)90024-3
M3 - Article
AN - SCOPUS:49149147203
VL - 9
SP - 238
EP - 247
JO - Bioorganic Chemistry
JF - Bioorganic Chemistry
SN - 0045-2068
IS - 2
ER -