Kinetic analysis of proton translocation catalyzed by F0F1 ATPase

FEBS Letters

Hirata, Hajime¹  Muneyuki, Eiro² 

[1]Department of Biochemistry,Jichi Medical School, Minami-Kawachi machi, Kawachi-gun, Tochigi 329-04, Japan

[2]Department of Biochemistry and Biophysics, Faculty of Science, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113, Japan

关键词: F0F1-ATPase;    Proton translocation;    Alternate binding change model;    Negative cooperativity;    (Submitochondrial particle);    SMP;    submitochondrial particle;    ANS;    8-anilino-naphthalene-1-sulfonate;    ED;    an enzyme which binds ADP and Pi;    EDT;    an enzyme which binds ATP;    ADP and Pi;    EDTD;    an enzyme which binds two ADPs;    Pis and ATP;    E*DTD;    the energized form of EDTD;   

DOI  :  10.1016/0014-5793(88)80137-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Kinetic analysis of both proton translocating and steady-state ATP hydrolytic activities catalyzed by F₀F₁ ATPase in submitochondrial particles were carried out over an ATP concentration range of 1–2000 μM. The results were examined in relation to the prediction based on the alternate binding change model proposed by Gresser et al. [(1982) J. Biol. Chem. 257, 12030–12038] in which energy transduction occurs only at the tri-site catalytic cycle. The present results essentially contrast with the model and rather indicate that if the alternate binding mechanism holds for the ATP hydrolytic reaction, the proton translocation should be coupled to at least both bi-site tri-site cycles.

【 授权许可】

Unknown