期刊
FEBS LETTERS
卷 589, 期 11, 页码 1194-1199出版社
WILEY-BLACKWELL
DOI: 10.1016/j.febslet.2015.03.029
关键词
Hydrogen/deuterium exchange; Cellobiose dehydrogenase; Calcium effect; Interdomain electron transfer; Flavocytochrome; Electrostatic interaction
资金
- Czech Science Foundation [P206/12/0503]
- Charles University [UNCE_204025/2012]
- European funds [CZ.1.07/2.3.00/20.0055, CZ.1.05/1.1.00/02.0109]
- Austrian Academy of Sciences
Cellobiose dehydrogenase (CDH) from wood degrading fungi represents a subclass of oxidoreductases with unique properties. Consisting of two domains exhibiting interdomain electron transfer, this is the only known flavocytochrome involved in wood degradation. High resolution structures of the separated domains were solved, but the overall architecture of the intact protein and the exact interface of the two domains is unknown. Recently, it was shown that divalent cations modulate the activity of CDH and its pH optimum and a possible mechanism involving bridging of negative charges by calcium ions was proposed. Here we provide a structural explanation of this phenomenon confirming the interaction between negatively charged surface patches and calcium ions at the domain interface. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据