ATP‐driven rotation of the γ subunit in F1‐ATPase

FEBS Letters

Nadanaciva, Sashi¹  Senior, Alan E¹  Weber, Joachim¹ 

[1] Department of Biochemistry and Biophysics, Box 712, University of Rochester Medical Center, Rochester, NY 14642, USA

关键词: ATP synthase;    ATP synthesis;    ATP hydrolysis;    Rotation;    Nucleotide binding;   

DOI  :  10.1016/S0014-5793(00)02071-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We present a mechanism for F₁-ATPase in which hydrolysis of MgATP in the high-affinity catalytic site at the α/β interface drives rotation of the γ subunit via conformational changes in the α subunit. During hydrolysis, transition state formation and separation of P_i from MgADP causes movement of portions of α, transmitted via two Arg residues which are hydrogen-bonded to the γ-phosphate of MgATP, αArg376 and βArg182; the latter is also hydrogen-bonded to interfacial α residues between α346 and α349. Changes in α conformation then push on γ, resulting in rotation. Supporting evidence from the literature and from new data is discussed.

【 授权许可】

Unknown