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Iron-containing urease in a pathogenic bacterium

机译:病原菌中的含铁脲酶

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摘要

Helicobacter mustelae, a gastric pathogen of ferrets, synthesizes a distinct iron-dependent urease in addition to its archetypical nickel-containing enzyme. The iron-urease is oxygen-labile, with the inactive protein exhibiting a methemerythrin-like electronic spectrum. Significantly, incubation of the oxidized protein with dithionite under anaerobic conditions leads to restoration of activity and bleaching of the spectrum. Structural analysis of the oxidized species reveals a dinuclear iron metallocenter bridged by a lysine carbamate, closely resembling the traditional nickel-urease active site. Although the iron-urease is less active than the nickel-enzyme, its activity allows H. mustelae to survive the carnivore's low-nickel gastric environment.
机译:雪貂的幽门螺杆菌是雪貂的一种胃病原体,除了其典型的含镍酶外,还合成了一种独特的铁依赖性脲酶。铁脲酶是氧不稳定的,非活性蛋白表现出类似四氢菊酯的电子光谱。明显地,在厌氧条件下将氧化的蛋白质与连二亚硫酸盐一起孵育导致活性恢复和光谱漂白。氧化物种的结构分析显示,赖氨酸氨基甲酸酯桥接了一个双核金属中心,非常类似于传统的镍脲酶活性位点。尽管铁脲酶的活性不如镍酶,但它的活性使H. mustelae能够在食肉动物的低镍胃环境中生存。

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