Abstract: 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.