Abstract
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.
Original language | English |
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Pages (from-to) | 238-247 |
Number of pages | 10 |
Journal | Bioorganic Chemistry |
Volume | 9 |
Issue number | 2 |
DOIs | |
Publication status | Published - Jan 1 1980 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Drug Discovery
- Organic Chemistry
Cite this
A flavoenzyme model : Facile oxidation of thiols by a flavin immobilized in cationic polyelectrolytes. / Shinkai, Seiji; Yamada, Shinji; Ando, Reiko; Kunitake, Toyoki.
In: Bioorganic Chemistry, Vol. 9, No. 2, 01.01.1980, p. 238-247.Research output: Contribution to journal › Article
}
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
PY - 1980/1/1
Y1 - 1980/1/1
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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UR - http://www.scopus.com/inward/citedby.url?scp=49149147203&partnerID=8YFLogxK
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 -