对铜蛋白质体蓝素中电子转移的核磁共振研究。

An NMR investigation of electron transfer in the copper-protein, plastocyanin.

Beattie J K, Fensom D J, Freeman H C, Woodcock E, Hill H A, Stokes A M

Biochim Biophys Acta. 1975 Sep 9;405(1):109-14. doi: 10.1016/0005-2795(75)90320-7.

Abstract

The proton NMR spectra of oxidised and reduced French bean plastocyanin have been recorded on a 270 MHz pulsed spctrometer. 2. The spectrum of a mixture containing the protein in the paramagnetic Cu(II) and diamagnetic Cu(I) states is a superposition of the separate spectra. When ferrirate spectra. 3. The results show that self-exchange between Cu(II)- and Cu(I)-plastocyanin is slow on the NMR time scale (kex less than 2-10(4) M-1-s-1 at 50 degrees C), and that electron transfer in the presence of ferricyanide is rapid (k greater than 1-10(5) M-1-s-1).

摘要

已在一台270兆赫脉冲光谱仪上记录了氧化和还原的菜豆质体蓝素的质子核磁共振谱。2. 含有处于顺磁性铜（II）和抗磁性铜（I）状态的蛋白质的混合物的光谱是各单独光谱的叠加。当高铁酸盐光谱时。3. 结果表明，在核磁共振时间尺度上，铜（II）-质体蓝素和铜（I）-质体蓝素之间的自交换很慢（在50℃时，交换速率常数kex小于2×10⁴ M⁻¹·s⁻¹），并且在铁氰化物存在下电子转移很快（速率常数k大于1×10⁵ M⁻¹·s⁻¹）。