Dunham K R, Selman B R
J Biol Chem. 1981 Jan 10;256(1):212-8.
Illumination of chloroplast thylakoid membranes results in the activation of the light-triggered ATPase (coupling factor 1) and in exchange of tightly bound adenine nucleotides. The dark decay of the light-triggered ATPase activity is accelerated significantly by the addition of ADP. Both the decay of the ATPase activity and the rebinding of ADP appear to be rate limited by the same unimolecular step which is estimated to have a rate constant of 0.058 +/- 0.005 s-1. ADP is a noncompetitive inhibitor of the ATPase, if sufficient time for binding is allowed. The Kis for ADP inhibition of the ATPase is equivalent to the K0.5 for ADP binding to the nucleotide tight binding site (K0.5 = 2 +/- 1 microM). A kinetic model is proposed which suggests that the binding of one ADP to chloroplast coupling factor 1 inhibits three ATPase active sites.
叶绿体类囊体膜受光照会激活光触发ATP酶（偶联因子1）并导致紧密结合的腺嘌呤核苷酸发生交换。添加ADP会显著加速光触发ATP酶活性的暗衰减。ATP酶活性的衰减和ADP的重新结合似乎都受限于同一个单分子步骤，该步骤的速率常数估计为0.058±0.005 s⁻¹。如果给予足够的结合时间，ADP是ATP酶的非竞争性抑制剂。ADP抑制ATP酶的Kis等同于ADP结合到核苷酸紧密结合位点的K0.5（K0.5 = 2±1 microM）。提出了一个动力学模型，该模型表明一个ADP与叶绿体偶联因子1的结合会抑制三个ATP酶活性位点。
