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将ATP加到[Fe_4S_4(SPh)_4]~(2-)的DMF-H_2O溶液中,引起[Fe_4S_4(SPh)_4]~(2-)原子簇的氧化还原电位从-1.00±0.01伏移至-1.49±0.01伏,负移490mV左右;使[Fe_4S_4(SPh)_4]~(2-)原子簇的电子吸收光谱特征吸收强度明显降低;同时加速[Fe_4S_4(SPh)_4]~(2-)与亚甲蓝的氧化还原反应,这种加速效应比ADP明显,而ADP又比AMP明显得多。根据这些实验事实,可以认为ATP能以末端的γ-PO_4基团,或γPO_4和β-PO_4基团与[Fe_4S_4(SPh)_4]~(2-)原子簇络合或螯合,引起后者的配位场增大,提高电子的输出能力。本文还讨论了ATP与[Fe_4S_4SPh)_4]~(2-)原子簇的络合方式,进而探讨了ATP在固氮酶中的结合部位和作用机理。
Addition of ATP to the DMF-H 2 O solution of [Fe 4 S 4 (SPh) 4] 2- (2-) caused the redox potential of [Fe 4 O 4 (SPh) 4] 2- clusters to shift from -1.00 ± 0.01 V to -1.49 ± 0.01 V and a negative shift of about 490 mV. The electron absorption spectrum of [Fe_4S_4 (SPh) _4] ~ (2-) With methylene blue redox reaction, this acceleration effect than ADP obvious, and ADP again significantly more than AMP. Based on these experimental facts, it can be considered that ATP can complex or chelate with the [Fe_4S_4 (SPh) _4] ~ (2-) cluster with terminal γ-PO_4 groups or γPO_4 and β-PO_4 groups, The coordination field increases, improve the electronic output capacity. This paper also discusses the complexation of ATP with [Fe_4S_4SPh] _4] ~ (2-) clusters, and then explores the binding site and mechanism of ATP in nitrogenase.