A NOVEL TERMINAL OXIDASE, CYTOCHROME-BAA3 PURIFIED FROM AEROBICALLY GROWN PSEUDOMONAS-AERUGINOSA - IT SHOWS A CLEAR DIFFERENCE BETWEEN RESTING STATE AND PULSED STATE

被引:26
作者
FUJIWARA, T [1 ]
FUKUMORI, Y [1 ]
YAMANAKA, T [1 ]
机构
[1] TOKYO INST TECHNOL, FAC BIOSCI & BIOTECHNOL, DEPT LIFE SCI, MIDORI KU, YOKOHAMA, KANAGAWA 227, JAPAN
关键词
D O I
10.1093/oxfordjournals.jbchem.a123893
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
A novel type of cytochrome c oxidase was purified to homogeneity from Pseudomonas aeruginosa which was grown aerobically. The purified oxidase contained two molecules of heme a, two atoms of copper, and one molecule of protoheme per molecule. One of the two heme a molecules in the oxidase reacted with carbon monoxide, so that the enzyme was of baa3-type. The oxidase molecule was composed of three subunits with molecular weights of 38,000, 57,000, and 82,000. Although the oxidase oxidized ferrocytochrome c-550 obtained from the bacterial cells grown aerobically, the oxidizing activity was not high. The "resting form" and the "pulsed form" of the oxidase were observed clearly with this enzyme, and the transition from the resting form to the pulsed form was accompanied by a distinct change of the enzymatic activity. The difference in the kinetics of the catalytic reactions between the two forms is discussed.
引用
收藏
页码:290 / 298
页数:9
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