Uni‐site catalysis by Escherichia coli F1‐ATPase with different numbers of bound nucleotides

FEBS Letters

Futai, Masamitsu¹  Hanada, Hironori¹  Maeda, Masatomo¹  Noumi, Takato¹ 

[1] Department of Organic Chemistry and Biochemistry, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567, Japan

关键词: ATPase;    H+-;    F1;    Uni-site catalysis;    Bound nucleotide;    (Escherichia coli);   

DOI  :  10.1016/0014-5793(89)81597-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We prepared two types of E. coli F₁ by slightly different gel filtration procedures of the purified F₁: F₁(II) contained about 2 mol, and F₁(V) about 5 mol of bound adenine nucleotides per mol of the enzyme. Thus F₁(II) had more than 2, possibly 3, vacant catalytic sites, while F₁(V) had less than one vacant catalytic site. The rate of ATP hydrolysis in uni-site catalysis (in the presence of inorganic phosphate) was about 3-fold higher with F₁(II) than with F₁(V), suggesting that ADP and inorganic phosphate bound at the catalytic sites of F₁(V) changed the kinetics of uni-site catalysis significantly.

【 授权许可】

Unknown