Amzel L M, Bianchet M A, Pedersen P L
Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, Maryland 21205.
J Bioenerg Biomembr. 1992 Oct;24(5):429-33. doi: 10.1007/BF00762358.
It has been proposed that during ATP synthesis/hydrolysis F1 ATPases experience a complex pattern of nucleotide binding and release during the catalytic cycle (binding change mechanism). This type of mechanism has implications that can be correlated with the structure of the enzyme. F1-ATPases (stoichiometry alpha 3 beta 3 gamma delta epsilon) are essentially a symmetrical trimer of pairs of the major subunits (alpha and beta); the minor subunits (gamma, delta and epsilon) are in single copies and interact with the trimer in an asymmetrical fashion. The asymmetry introduced by the minor subunits has important structural and functional consequences: (1) it introduces differences between the potentially equivalent binding and catalytic sites in the major subunits, (2) it restricts the ways in which a binding change mechanism can occur, and (3) it governs the way in which the F1 interacts with the (asymmetrical) F0 sector.
有人提出，在ATP合成/水解过程中，F1 ATP酶在催化循环中经历了复杂的核苷酸结合和释放模式（结合变化机制）。这种机制具有一些与酶的结构相关的含义。F1-ATP酶（化学计量比为α3β3γεδ）本质上是主要亚基（α和β）对的对称三聚体；次要亚基（γ、δ和ε）为单拷贝，并以不对称方式与三聚体相互作用。次要亚基引入的不对称性具有重要的结构和功能后果：（1）它在主要亚基中潜在等效的结合和催化位点之间引入差异，（2）它限制了结合变化机制可能发生的方式，（3）它控制着F1与（不对称的）F0部分相互作用的方式。
