Püttner I, Solioz M, Carafoli E, Ludwig B
Eur J Biochem. 1983 Jul 15;134(1):33-7. doi: 10.1111/j.1432-1033.1983.tb07527.x.
The effect of dicyclohexylcarbodiimide (DCCD) on the proton pumping two-subunit cytochrome c oxidase from Paracoccus denitrificans was investigated. Purified Paracoccus oxidase was reconstituted into phospholipid vesicles by cholate dialysis. Following incubation with increasing amounts of DCCD, proton ejection was recorded in response to reductant pulses with reduced cytochrome c. Concentrations of DCCD which greatly reduced proton pumping by bovine cytochrome c oxidase used as a control were found to exert only a minor effect on proton translocation by Paracoccus oxidase. Similarly, incubation of the bacterial enzyme with [14C]DCCD failed to reveal the specific covalent interaction previously demonstrated to occur with bovine cytochrome c oxidase, and here also shown for the oxidase of yeast. Thus, Paracoccus oxidase differs in its interaction with DCCD from the functionally analogous eukaryotic enzymes.
研究了二环己基碳二亚胺（DCCD）对反硝化副球菌质子泵浦双亚基细胞色素c氧化酶的影响。通过胆酸盐透析将纯化的副球菌氧化酶重构到磷脂囊泡中。用越来越多的DCCD孵育后，记录用还原型细胞色素c进行还原剂脉冲时的质子排出情况。用作对照的牛细胞色素c氧化酶中，能极大降低质子泵浦作用的DCCD浓度，对副球菌氧化酶的质子转运仅产生轻微影响。同样，用[14C]DCCD孵育该细菌酶，未能揭示先前证明与牛细胞色素c氧化酶发生的特异性共价相互作用，此处酵母氧化酶也显示有这种相互作用。因此，副球菌氧化酶与DCCD的相互作用不同于功能类似的真核酶。
