Laser flash photolysis studies of the kinetics of reduction of ferredoxins and ferredoxin-NADP+ reductases from Anabaena PCC 7119 and spinach: electrostatic effects on intracomplex electron transfer.
Laser flash photolysis studies of the kinetics of reduction of ferredoxins and ferredoxin-NADP+ reductases from Anabaena PCC 7119 and spinach: electrostatic effects on intracomplex electron transfer.
复制标题
鱼腥藻 PCC 7119 和菠菜中铁氧还蛋白和铁氧还蛋白-NADP 还原酶还原动力学的激光闪光光解研究:静电对复合物内电子转移的影响。
DOI:
10.1016/0003-9861(91)90489-6
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发表时间:
1991
影响因子:
3.9
通讯作者:
Tollin,G
中科院分区:
文献类型:
--
作者:
Walker,MC;Pueyo,JJ;Navarro,JA;Gómez-Moreno,C;Tollin,G
The influence of electrostatic forces on the formation of, and electron transfer within, transient complexes between redox proteins was examined by comparing ionic strength effects on the kinetics of the electron transfer reaction between reduced ferredoxins (Fd) and oxidized ferredoxin-NADP+reductases (FNR) fromAnabaenaand from spinach, using laser flash photolysis techniques. With theAnabaenaproteins, direct reduction by laser-generated flavin semiquinone of the FNR component was inhibited by complex formation at low ionic strength, whereas Fd reduction was not. The opposite results were obtained with the spinach system. These observations clearly indicate structural differences between the cyanobacterial and higher plant complexes. For the complex formed by theAnabaenaproteins, the results indicate that electrostatic forces are not a major contributor to complex stability. However, the rate constant for intracomplex electron transfer had a biphasic dependence on ionic strength, suggesting that structural rearrangements within the transient complex facilitate electron transfer. In contrast to theAnabaenacomplex, electrostatic forces are important for the stabilization of the spinach Fd:FNR complex, and changes in ionic strength had little effect on the limiting rate constant for intracomplex electron transfer. This suggests that in this case the geometry of the initial collisional complex is optimal for reaction. These results provide a clear illustration of the differing roles that electrostatic interactions may play in controlling electron transfer between two redox proteins.