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首页> 外文期刊>The FEBS journal >Agrobacterium tumefaciens type II NADH dehydrogenase. Characterization and interactions with bacterial and thylakoid membranes
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Agrobacterium tumefaciens type II NADH dehydrogenase. Characterization and interactions with bacterial and thylakoid membranes

机译：根癌农杆菌II型NADH脱氢酶。细菌膜和类囊体膜的表征及其相互作用

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摘要

Type II NADH dehydrogenases (NDH-2) are monomeric enzymes that catalyse quinone reduction and allow electrons to enter the respiratory chain in different organisms including higher plant mitochondria, bacteria and yeasts. In this study, an Agrobacterium tumefaciens gene encoding a putative alternative NADH dehydrogenase (AtuNDH-2) was isolated and expressed in Escherichia coli as a (His)6-tagged protein. The purified 46 kDa protein contains FAD as a prosthetic group and oxidizes both NADH and NADPH with similar Vmax values, but with a much higher affinity for NADH than for NADPH. AtuNDH-2 complements the growth (on a minimal medium) of an E. coli mutant strain deficient in both NDH-1 and NDH-2, and is shown to supply electrons to the respiratory chain when incubated with bacterial membranes prepared from this mutant. By measuring photosystem II chlorophyll fluorescence on thylakoid membranes prepared from the green alga Chlamydomonas reinhardtii, we show that AtuNDH-2 is able to stimulate NADH-dependent reduction of the plastoquinone pool. We discuss the possibility of using heterologous expression of NDH-2 enzymes to improve nonphotochemical reduction of plastoquinones and H2 production in C. reinhardtii.
机译：II型NADH脱氢酶（NDH-2）是催化醌还原并允许电子进入不同生物（包括高等植物线粒体，细菌和酵母菌）的呼吸链的单体酶。在这项研究中，农杆菌介导的基因编码假定的替代NADH脱氢酶（AtuNDH-2）被分离，并在大肠杆菌中表达为（His）6-tagged蛋白。纯化的46 kDa蛋白包含FAD作为辅基，并以相似的Vmax值氧化NADH和NADPH，但对NADH的亲和力比对NADPH的亲和力高得多。 AtuNDH-2补充了缺乏NDH-1和NDH-2的大肠杆菌突变菌株的生长（在基本培养基上），当与由该突变株制备的细菌膜孵育时，AtuNDH-2被证明可为呼吸链提供电子。通过测量由绿藻莱茵衣藻制备的类囊体膜上的光系统II叶绿素荧光，我们显示AtuNDH-2能够刺激NADH依赖性的质体醌库还原。我们讨论了使用NDH-2酶的异源表达来改善莱茵衣藻中质体醌的非光化学还原和H2产生的可能性。

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