蓝细菌中固氮酶的一种新型共价修饰。

A novel covalent modification of nitrogenase in a cyanobacterium.

作者信息

Gallon J R, Cheng J, Dougherty L J, Gallon V A, Hilz H, Pederson D M, Richards H M, Rüggeberg S, Smith C J

机构信息

Biochemistry Research Group, School of Biological Sciences, University of Wales Swansea, Singleton Park, Swansea, UK.

出版信息

FEBS Lett. 2000 Feb 25;468(2-3):231-3. doi: 10.1016/s0014-5793(00)01229-1.

DOI:10.1016/s0014-5793(00)01229-1

PMID:10692592

Abstract

In extracts of the unicellular cyanobacterium Gloeothece, the Fe-protein of nitrogenase can be separated by SDS-PAGE into two antigenically identifiable components. Unlike the situation in photosynthetic bacteria such as Rhodospirillum rubrum, these two forms do not arise from covalent modification of the protein by ADP-ribosylation. Rather, the Fe-protein of Gloeothece nitrogenase is subjected to modification by palmitoylation.

摘要

在单细胞蓝细菌聚球藻的提取物中，固氮酶的铁蛋白可通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）分离为两种抗原可识别的组分。与诸如深红红螺菌等光合细菌的情况不同，这两种形式并非由蛋白质经ADP-核糖基化的共价修饰产生。相反，聚球藻固氮酶的铁蛋白会受到棕榈酰化修饰。