The Structure of the ADP•AlF4- stabilized nitrogenase complex and its implications for signal transduction mechanism
The Structure of the ADP•AlF4- stabilized nitrogenase complex and its implications for signal transduction mechanism
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ADP·AlF4稳定固氮酶复合物的结构及其对信号转导机制的影响
DOI：
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发表时间：
1997
期刊：
影响因子：
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通讯作者：
D. Rees
中科院分区：
文献类型：
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作者：
H. Schindelin;C. Kisker;J. Schlessman;J. Howard;D. Rees
生物固氮过程中，ATP水解酶与固氮酶的电子传递偶联是核苷酸依赖的信号转导机制的一个重要例子。由ADP·AIF4-稳定的固氮酶的铁蛋白和钼蛋白之间的络合物的晶体结构已经确定。ADP·AIF4-以前是核苷酸开关蛋白中的核苷三磷酸类似物。该结构揭示了二聚体铁蛋白发生了实质性的构象变化。β-磷酸和AIF4-基团通过对催化至关重要的亚基间接触来稳定，氧化还原中心被重新定位以促进电子转移。固氮酶复合体中的相互作用对多蛋白复合体中的信号和能量转导机制具有广泛的意义。
The coupling of ATP hydrolysis to electron transfer by the enzyme nitrogenase during biological nitrogen fixation is an important example of a nucleotide-dependent transduction mechanism. The crystal structure has been determined for the complex between the Fe-protein and MoFe-protein components of nitrogenase stabilized by ADP·AIF4–, previously used as a nucleoside triphosphate analogue in nucleotide-switch proteins. The structure reveals that the dimeric Fe-protein has undergone substantial conformational changes. The β-phosphate and AIF4– groups are stabilized through intersubunit contacts that are critical for catalysis and the redox centre is repositioned to facilitate electron transfer. Interactions in the nitrogenase complex have broad implications for signal and energy transduction mechanisms in multiprotein complexes.