首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor
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Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor

机译:金属运输以固氮:NifQ向NifEN / NifH捐赠钼,用于生物合成固氮酶FeMo-辅因子

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摘要

The molybdenum nitrogenase, present in a diverse group of bacteria and archea, is the major contributor to biological nitrogen fixation. The nitrogenase active site contains an iron-molybdenum cofactor (FeMo-co) composed of 7Fe, 9S, 1Mo, one unidentified light atom, and homocitrate. The nifQ gene was known to be Involved in the incorporation of molybdenum into nitrogenase. Here we show direct biochemical evidence for the role of NifQ in FeMo-co biosynthesis. As-isolated NifQ was found to carry a molybdenum-iron-sulfur cluster that serves as a specific molybdenum donor for FeMo-co biosynthesis. Purified NifQ supported in vitro FeMo-co synthesis in the absence of an additional molybdenum source. The mobilization of molybdenum from NifQ required the simultaneous participation of NifH and NifEN in the in vitro FeMo-co synthesis assay, suggesting that NifQ would be the physiological molybdenum donor to a hypothetical NifEN/NifH complex.
机译:存在于多种细菌和古细菌中的钼固氮酶是生物固氮的主要贡献者。固氮酶活性位点包含由7Fe,9S,1Mo,一个未确定的轻原子和纯柠檬酸盐组成的铁钼辅因子(FeMo-co)。已知nifQ基因参与将钼掺入固氮酶中。在这里,我们显示了NifQ在FeMo-co生物合成中的作用的直接生化证据。发现分离出的NifQ带有钼铁硫簇,可作为FeMo-co生物合成的特定钼供体。在没有其他钼源的情况下,纯化的NifQ支持体外FeMo-co合成。从NifQ迁移钼需要NifH和NifEN同时参与体外FeMo-co合成测定,这表明NifQ将是假设的NifEN / NifH复合物的生理钼供体。

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