Purification characterization of the inhibitory subunit (δ) of the ATP‐synthase from Micrococcus luteus

FEBS Letters

Dose, Klaus¹  Junge, Wolfgang²  Engelbrecht, Siegfried²  Grüber, Gerhard¹  Nawroth, Thomas¹ 

[1] Institut für Biochemie, Joh. Gutenberg-Universität, Becherweg 30, 55099 Mainz, Germany;Biophysik, Fachberich Biologie/Chemie, Universität Osnabrück, 49069 Osnabrück, Germany

关键词: ATP-synthase;    Micrococcus luteus;    CF1;    δ subunit;    ε subunit;    Inhibitor protein;    Reconstitution;    ATP-synthase (EC3.6.1.34) from M. luteus;    ATP-synthase (−δ);    ATP-synthase lacking the δ-subunit;    F0;    F0 complex of ATP-synthase;    F0;    F1subcomplex of ATP-synthase;    CF1;    chloroplast ATPase;    CF0;    chloroplast proton channel;    CF1-ε;    ε subunit of chloroplast ATPase;   

DOI  :  10.1016/0014-5793(94)01271-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Subunit δ was isolated from the ATP-synthase from Micrococcus luteus strain (ATCC 4698). δ, in the case of M. luteus F₀F₁-ATPase, acts as an inhibitor of ATP hydrolysis and thus resembles subunits in E. coli and chloroplast ATP-synthase. After treatment with 1.5 M LiCl the ATP-synthase dissociated, and subsequently subunit δ (27 kDa) was purified by hydrophobic interaction chromatography. Inhibition of ATP-synthase lacking δ by addition of δ showed noncompetitive kinetics with a K _i of ∼ 5.9nM. Subunit ε from chloroplast F₁, which corresponds functionally to the M. luteus F₀F₁-δ, and chloroplast δ were tested for ATPase inhibitory activity by addition to the partially δ-depleted ATP-synthase from M. luteus. CF₁-ε inhibited M. luteus ATP-synthase up to 80%, whereas CF₁-δ did not show any influence.

【 授权许可】

Unknown