Stoner C D, Sirak H D
J Cell Biol. 1973 Jan;56(1):65-73. doi: 10.1083/jcb.56.1.65.
In bovine heart mitochondria bongkrekic acid at concentrations as low as about 4 nmol/mg protein (a) completely inhibits phosphorylation of exogenous adenosine diphosphate (ADP) and dephosphorylation of exogenous adenosine triphosphate (ATP), (b) completely reverses atractyloside inhibition of inner membrane contraction induced by exogenous adenine nucleotides, and (c) decreases the amount of adenine nucleotide required to elicit maximal exogenous adenine nucleotide-induced inner membrane contraction to a level which appears to correspond closely with the concentration of contractile, exogenous adenine nucleotide binding sites Bongkrekic acid at concentrations greater than 4 nmol/mg protein induces inner membrane contraction which seems to depend on the presence of endogenous ADP and/or ATP. The findings appear to be consistent with the interpretations (a) that the inner mitochondrial membrane contains two types of contractile, adenine nucleotide binding sites, (b) that the two sites differ markedly with regard to adenine nucleotide affinity, (c) that the high affinity site is identical with the adenine nucleotide exchange carrier, (d) that the low affinity site is accessible exclusively to endogenous adenine nucleotides and is largely unoccupied in the absence of bongkrekic acid, and (e) that bongkrekic acid increases the affinity of both sites in proportion to the amount of the antibiotic bound to the inner membrane.
在牛心线粒体中，浓度低至约4 nmol/mg蛋白质的邦克里酸（a）完全抑制外源性二磷酸腺苷（ADP）的磷酸化和外源性三磷酸腺苷（ATP）的去磷酸化，（b）完全逆转苍术苷对外源性腺嘌呤核苷酸诱导的内膜收缩的抑制作用，并且（c）将引发最大外源性腺嘌呤核苷酸诱导的内膜收缩所需的腺嘌呤核苷酸量降低到一个似乎与收缩性外源性腺嘌呤核苷酸结合位点的浓度密切对应的水平。浓度大于4 nmol/mg蛋白质的邦克里酸诱导内膜收缩，这似乎取决于内源性ADP和/或ATP的存在。这些发现似乎与以下解释一致：（a）线粒体内膜含有两种收缩性腺嘌呤核苷酸结合位点；（b）这两个位点在腺嘌呤核苷酸亲和力方面有显著差异；（c）高亲和力位点与腺嘌呤核苷酸交换载体相同；（d）低亲和力位点仅对内源性腺嘌呤核苷酸可及，并且在不存在邦克里酸的情况下大部分未被占据；以及（e）邦克里酸按与结合到内膜上的抗生素量成比例地增加两个位点的亲和力。
