Hughes J B, Joshi S, Sanadi D R
J Biol Chem. 1982 Jun 25;257(12):6697-701.
Bovine mitochondrial coupling factor B (FB) stimulates oxidative phosphorylation as well as other energy-linked reactions which are supported by ATP hydrolysis. Extraction of FB from submitochondrial particles results in a decrease in ATP-dependent proton translocation (delta pH) and binding of the voltage-sensitive dye, oxonol VI. Reconstitution of deficient particles with FB restores ATP-dependent proton translocation and oxonol binding but has little effect on oxonol binding supported by respiratory substrates.l In contrast, low levels of oligomycin stimulate oxonol binding supported by either ATP or NADH. In the case of oligomycin, the stimulatory effect is associated with a decrease in the rate of discharge of the proton gradient, but the depletion of FB or its restoration has no detectable effect on the discharge rate. The data indicate that the primary effect of FB is upon the rate of H+ translocation coupled to ATP hydrolysis, while that of low oligomycin is on the H+ permeability of the membrane.
牛线粒体偶联因子B（FB）可刺激氧化磷酸化以及其他由ATP水解支持的能量相关反应。从亚线粒体颗粒中提取FB会导致ATP依赖性质子转运（ΔpH）以及电压敏感染料奥克诺尔VI的结合减少。用FB重建缺陷颗粒可恢复ATP依赖性质子转运和奥克诺尔结合，但对呼吸底物支持的奥克诺尔结合影响很小。相反，低水平的寡霉素会刺激由ATP或NADH支持的奥克诺尔结合。就寡霉素而言，刺激作用与质子梯度的放电速率降低有关，但FB的耗尽或恢复对放电速率没有可检测到的影响。数据表明，FB的主要作用是对与ATP水解偶联的H+转运速率，而低剂量寡霉素的作用是对膜的H+通透性。
