固氮酶活性中心模型化合物的合成和性质的研究——一种具有生物组合活性的原子簇化合物

在这篇文章中,我们报道了一种具有生物组合活性的固氮酶活性中心模型化合物的合成、光谱性质、催化活性和生物组合性质。以KBH₄为还原剂,该化合物的乙炔还原活性达11.11nM产物/nM·Mo·分钟,对乙烯的选择性为74.8%。¹⁵N标记实验表明,它具有一定周氮活性。与柱分离的缺辅基钼铁蛋白组合加铁蛋白,乙炔还原活性高达38.21nM乙烯/nMMo分钟,相当于天然FeMo-co活性的9%。缺辅基钼铁蛋白与模型化合物组合聚丙烯酰胺凝胶电泳迁移率比组合前更加接近正常钼铁蛋白的电泳迁移率。

SYNTHESIS AND PROPERTY STUDY OF A MODEL COMPOUND OF ACTIVE CENTER OF NITROGENASE

In this paper, we report the synthesis, spectra properties, catalytic activity and reconstitution properties of a model compound of active center of nitrogenase, which displays good reconstitution behaviour with inactive FeMo protein from azotobacter vinelandii mutant strain UW45. The turnover of acetylene reduction with present compound as catalyst and KBH4 as reductant is 11.11nM products/nMMo·min. Selectivity to ethylene is 74.8%.15N labeled experiment shows that it displays appreciable activity to reduce 15N2 to 15NH3. The activity of acetylene reduction upon reconstitution of this compound with inactive FeMo protein and addition of Fe protein is high as 38.1 nMC2 H4/nMMo·min., equaling to 9% of that of nitrogenase. The electrophoretic mobility after reconstitution of inactive FeMo protein with the model compound is closer to that of normal FeMo protein than reconstitution before.