Nicholas R A, Ordal G W
Biochem J. 1978 Dec 15;176(3):639-47. doi: 10.1042/bj1760639.
Analogues of the potent uncoupler of oxidative phosphorylation pentachlorophenol were tested as inhibitors of proline and glycine transport by Bacillus subtilis. These analogues included less highly substituted chlorophenols and pentachlorothiophenol. Like pentachlorophenol, they are non-competitive inhibitors of proline transport and uncompetitive inhibitors of glycine transport. However, the less highly substituted chlorophenols are weaker acids than pentachlorophenol and also weaker inhibitors. Analysis indicated that the anionic form of the uncouplers is the inhibiting species. Pentachlorothiophenol, a water-insoluble anion, is also a potent inhibitor. These results support previous studies that concluded that uncouplers of oxidative phosphorylation inhibit amino acid transport by binding at specific sites on proteins, the free energy of interaction stabilizing 'unproductive' conformations. Such specific interactions of uncoupler with protein are probably commonplace.
对氧化磷酸化的强效解偶联剂五氯苯酚的类似物进行了测试，以考察其作为枯草芽孢杆菌脯氨酸和甘氨酸转运抑制剂的效果。这些类似物包括取代程度较低的氯酚和五氯硫酚。与五氯苯酚一样，它们是脯氨酸转运的非竞争性抑制剂和甘氨酸转运的反竞争性抑制剂。然而，取代程度较低的氯酚酸性比五氯苯酚弱，也是较弱的抑制剂。分析表明，解偶联剂的阴离子形式是起抑制作用的物种。五氯硫酚是一种水不溶性阴离子，也是一种强效抑制剂。这些结果支持了先前的研究，该研究得出结论，氧化磷酸化的解偶联剂通过结合在蛋白质上的特定位点来抑制氨基酸转运，相互作用的自由能稳定了“非生产性”构象。解偶联剂与蛋白质的这种特异性相互作用可能很常见。
