NB-protein (BchN-BchB) of dark-operative protochlorophyllide reductase is the catalytic component containing oxygen-tolerant Fe-S clusters
NB-protein (BchN-BchB) of dark-operative protochlorophyllide reductase is the catalytic component containing oxygen-tolerant Fe-S clusters
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DOI：
10.1016/j.febslet.2008.03.018
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发表时间：
2008-04-16
期刊：
影响因子：
3.5
通讯作者：
Fujita, Yuichi
中科院分区：
文献类型：
--
作者：
Nomata, Jiro;Ogawa, Takuro;Fujita, Yuichi
暗操作原叶绿内酯（Pchlide）氧化还原酶是一种由l蛋白（bchl -二聚体）和nb蛋白（BchN - bchb -异四聚体）两种组分组成的类氮素酶。在这里，我们发现nb蛋白是具有Fe -S簇的催化成分。从荚膜红杆菌结合的Pchlide中纯化的nb蛋白，在加入l蛋白和MgATP后容易转化为叶绿素内酯a。nb蛋白的抗暴露活性较强。从缺乏bchh的突变体中纯化的无pchlide形式的nb蛋白显示出吸收光谱，表明存在Fe -S中心。结合铁和硫化物含量，这些发现表明nb蛋白携带两个耐氧[4Fe-4S]簇。(C) 2008年欧洲生化学会联合会。Elsevier b.v.版权所有。
Dark-operative protochlorophyllide (Pchlide) oxidoreductase is a nitrogenase-like enzyme consisting of the two components, L-protein (BchL-dimer) and NB-protein (BchN -BchB-heterotetramer). Here, we show that NB-protein is the catalytic component with Fe -S clusters. NB-protein purified from Rhodobacter capsulatus bound Pchlide that was readily converted to chlorophyllide a upon the addition of L-protein and MgATP. The activity of NB-protein was resistant to the exposure to air. A Pchlide-free form of NB-protein purified from a bchH-lacking mutant showed an absorption spectrum suggesting the presence of Fe -S centers. Together with the Fe and sulfide contents, these findings suggested that NB-protein carries two oxygen-tolerant [4Fe-4S] clusters. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.