Konishi K, Adachi H, Kita K, Horikoshi I
Department of Biochemistry, Faculty of Medicine, Toyama Medical and Pharmaceutical University, Japan.
Chem Pharm Bull (Tokyo). 1990 Feb;38(2):474-6. doi: 10.1248/cpb.38.474.
The effects of pentagalloylglucose (1,2,3,4,6-penta-O-galloyl-beta-D-glucose) on the aerobic electron transport system of Escherichia coli were studied. The activity of nicotineamide adenine dinucleotide (NADH) reductase was inhibited by pentagalloylglucose, but the activities of succinate dehydrogenase, D-lactate dehydrogenase, and ubiquinol-1 (Q1H2) oxidase were not susceptible to the inhibitor. Because the presence of two kinds of NADH dehydrogenase in respiratory chain of Escherichia coli has been reported, we examined the effect of galloylglucose independently on both NADH dehydrogenases. Pentagalloylglucose is potent and specific inhibitor of both NADH dehydrogenases. One of the NADH dehydrogenases (NADH dh II) is more sensitive to the inhibitor than the other (NADH dh I).
研究了五倍没食子酰葡萄糖(1,2,3,4,6 - 五 - O - 没食子酰 - β - D - 葡萄糖)对大肠杆菌有氧电子传递系统的影响。五倍没食子酰葡萄糖抑制了烟酰胺腺嘌呤二核苷酸(NADH)还原酶的活性,但琥珀酸脱氢酶、D - 乳酸脱氢酶和泛醇 - 1(Q1H2)氧化酶的活性对该抑制剂不敏感。由于已报道大肠杆菌呼吸链中存在两种NADH脱氢酶,我们分别研究了没食子酰葡萄糖对这两种NADH脱氢酶的影响。五倍没食子酰葡萄糖是两种NADH脱氢酶的强效特异性抑制剂。其中一种NADH脱氢酶(NADH dh II)比另一种(NADH dh I)对该抑制剂更敏感。