Monoclonal antibodies to cytochrome c from Paracoccus denitrificans: effects on electron transport reactions.

Monoclonal antibodies to cytochrome c from Paracoccus denitrificans: effects on electron transport reactions.
复制标题

来自脱氮副球菌的细胞色素 c 单克隆抗体:对电子传递反应的影响。

DOI:
10.1016/0005-2728(85)90189-6
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发表时间:
1985
期刊:
Biochimica et biophysica acta
影响因子:
--
通讯作者:
Smith,L
Smith,L
中科院分区:
--
文献类型:
--
作者:
Kuo,LM;Davies,HC;Smith,L

文献摘要

相似文献

The effect of a monoclonal antibody to a soluble cytochromecfromParacoccus denitrificanswas tested on the membrane-bound electron-transport system of this bacterium. This antibody (F3-10.2) and one previously described (F3-29.4) (Kuo, L.M., Davies, H.C. and Smith, L. (1984) Biochim. Biophys. Acta 766, 472–482) were deduced to bind to the cytochromecin the area including amino acid residue number 23 on a loop on the side of the heme crevice. In contrast to the observations with the previously tested antibody, the present data show the second antibody to block completely the reaction of the cytochromecwith cytochromecoxidase but not that with cytochromecreductase. Neither antibody has an appreciable inhibitory effect on the NADH oxidase of the isolated detergent-treated membranes. The two antibodies bind in different ways, giving insight into the interaction of a soluble protein with membrane-bound enzymes. The data indicate that the reaction sites on the cytochromecfor the oxidase and reductase moieties ofP. denitrificansare different. They also argue against the need for a dissociable cytochromeccomparable to that which functions on the mitochondrial inner membrane.