Persson B, Rydström J
Biochem Biophys Res Commun. 1987 Jan 30;142(2):573-8. doi: 10.1016/0006-291x(87)90312-3.
The effect of glutathione, glutathione disulfide and the dithiol reagent phenylarsine oxide on purified soluble as well as reconstituted mitochondrial nicotinamide nucleotide transhydrogenase from beef heart was investigated. Glutathione disulfide and phenylarsine oxide caused an inhibition of transhydrogenase, the extent of which was dependent on the presence of either of the transhydrogenase substrates. In the absence of NADPH glutathione protected partially against inactivation by glutathione disulfide and phenylarsine oxide. In the presence of NADPH glutathione also inhibited transhydrogenase. Reconstituted transhydrogenase vesicles behaved differently as compared to the soluble transhydrogenase and was partially uncoupled by GSSG. It is concluded that transhydrogenase contains a dithiol that is essential for catalysis as well as for proton translocation.
研究了谷胱甘肽、二硫化谷胱甘肽和二硫醇试剂苯胂氧化物对纯化的可溶性以及重组的牛心线粒体烟酰胺核苷酸转氢酶的影响。二硫化谷胱甘肽和苯胂氧化物导致转氢酶受到抑制，其抑制程度取决于转氢酶底物之一的存在情况。在没有NADPH的情况下，谷胱甘肽可部分保护转氢酶免受二硫化谷胱甘肽和苯胂氧化物的失活作用。在有NADPH的情况下，谷胱甘肽也会抑制转氢酶。与可溶性转氢酶相比，重组转氢酶囊泡表现不同，并且会被GSSG部分解偶联。得出的结论是，转氢酶含有一种二硫醇，它对于催化以及质子转运至关重要。
