NifB-dependent in vitro synthesis of the iron-molybdenum cofactor of nitrogenase
NifB-dependent in vitro synthesis of the iron-molybdenum cofactor of nitrogenase
复制标题
DOI：
10.1073/pnas.0601115103
复制
发表时间：
2006-04-04
影响因子：
11.1
通讯作者：
Rubio, LM
中科院分区：
文献类型：
--
作者：
Curatti, L;Ludden, PW;Rubio, LM
生物固氮是支持地球上生命的生物地球化学氮循环的一个基本过程，由固氮酶催化。固氮酶活性中心含有一个由7Fe-9S-MoHomocitate组成的铁钼辅因子(FeMo-co)和一个尚未确定的原子，这可能是自然界中最复杂的[Fe-S]簇合物。在这里，我们展示了铁钼钴的简单成分，铁，S，钼，和高柠檬酸的体外合成。FEMO-co的体外合成需要纯化的NifB，依赖于S-腺苷蛋氨酸，这表明在FEMO-co组装过程中需要自由基化学。
Biological nitrogen fixation, an essential process of the biogeochemical nitrogen cycle that supports life on Earth, is catalyzed by the nitrogenase enzyme. The nitrogenase active site contains an iron and molybdenum cofactor (FeMo-co) composed of 7Fe-9S-Mohomocitrate and one not-yet-identified atom, which probably is the most complex [Fe-S] cluster in nature. Here, we show the in vitro synthesis of FeMo-co from its simple constituents, Fe, S, Mo, and homocitrate. The in vitro FeMo-co synthesis requires purified NifB and depends on S-adenosylmethionine, indicating that radical chemistry is required during FeMo-co assembly.