Quinoprotein alcohol dehydrogenase of acetic acid bacteria: Kinetic study on the enzyme purified from Acetobacter methanolicus

被引：13

作者：

Frebortova, J ^{[1
]}

Matsushita, K ^{[1
]}

Yakushi, T ^{[1
]}

Toyama, H ^{[1
]}

Adachi, O ^{[1
]}

机构：

[1] YAMAGUCHI UNIV, FAC AGR, DEPT BIOL CHEM, YAMAGUCHI 753, JAPAN

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1997年 / 61卷 / 03期

关键词：

quinoprotein; alcohol dehydrogenase; inhibition; reconstitution;

D O I：

10.1271/bbb.61.459

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An alcohol dehydrogenase (ADH) complex consisting of subunits I, II, and III and the free subunit II were purified from Acetobacter methanolicus. The kinetic parameters of the purified ADH were investigated with several artificial electron accepters, Simultaneous reactions with different electron accepters showed that these electron accepters competed with each other, Although free subunit II did not show any enzyme activity, part of the activity was restored after reconstitution with subunit I/III complex purified from Gluconobacter suboxydans, 2-n-Heptyl-4-hydroxyquinoline-N-oxide (HQNO) non-competitively inhibited all the reductase activities of native ADH, while the ferricyanide reductase activity of hybrid ADH was not inhibited by HQNO but the ubiquinone reductase activity was inhibited competitively, The kinetic study of native and hybrid ADHs suggests that at least three heme c moieties are involved in the reduction of ferricyanide and that the reduction of ubiquinone occurs in subunit II at a site different from the ferricyanide reacting site.

引用

页码：459 / 465

页数：7

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