Isolation of a novel NAD(P)H-quinone oxidoreductase from the cyanobacterium Synechocystis PCC6803.
Isolation of a novel NAD(P)H-quinone oxidoreductase from the cyanobacterium Synechocystis PCC6803.
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从蓝藻集胞藻 PCC6803 中分离出一种新型 NAD(P)H-醌氧化还原酶。
DOI：
10.1093/oxfordjournals.pcp.a029430
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发表时间：
1998
影响因子：
4.9
通讯作者：
K. Asada
中科院分区：
文献类型：
--
作者：
M. Matsuo;T. Endo;K. Asada
通过离子交换、亲和层析和凝胶过滤层析从蓝藻集胞藻6803中分离得到一种新的NAD（P）H-醌氧化还原酶（NQR）。分离的NQR被发现是一个drgA基因的产物，是一个同源二聚体组成的23 kDa的亚基。它显示出NAD（P）H-质体醌氧化还原酶活性，对NADPH和NADH的Km值分别为12和48 μ M。巯基修饰剂抑制活性，但不被鱼藤酮，异戊巴比妥，水杨羟肟酸，双香豆素，黄酮，或diphenyleniodonium氯化物。因此，Cys-147残基可能参与催化反应。纯化的NQR的氨基酸序列与NADH氧化酶、NAD（P）H-黄素氧化还原酶和硝基还原酶的氨基酸序列有一定的同源性，但不含腺嘌呤结合基序或磷酸结合基序，是一种新型的NQR。
A novel NAD(P)H-quinone oxidoreductase (NQR) was isolated from the cyanobacterium Synechocystis PCC6803 by ion-exchange, affinity and gel-filtration chromatographies. Isolated NQR was found to be a drgA gene product that was a homodimer composed of 23-kDa subunits. It showed NAD(P)H-plastoquinone oxidoreductase activity with Km values for NADPH and NADH of 12 and 48 microM, respectively. The activity was inhibited by thiolmodifying reagents, but not by rotenone, amobarbital, salicylhydroxamic acid, dicumarol, flavone, or diphenyleneiodonium chloride. Therefore, the Cys-147 residue is probably involved in the catalytic reaction. The amino acid sequence of the purified NQR had some homology with those of NADH oxidase, NAD(P)H-flavin oxidoreductase, and nitroreductase but did not contain either an adenine-binding motif or a phosphate-binding motif, thus, it is a new type of NQR.
嗜热栖热菌 HB-8 中两种类型的 NADH-醌还原酶的纯化和表征。
影响因子：
2.9
作者：
Yagi,T;Hon-nami,K;Ohnishi,T
通讯作者：
Ohnishi,T