NB-protein (BchN-BchB) of dark-operative protochlorophyllide reductase is the catalytic component containing oxygen-tolerant Fe-S clusters

被引：34

作者：

Nomata, Jiro ^{[1
]}

Ogawa, Takuro ^{[2
]}

Kitashima, Masaharu ^{[3
]}

Inoue, Kazuhito ^{[2
,3
]}

Fujita, Yuichi ^{[1
]}

机构：

[1] Nagoya Univ, Grad Sch Bioagr Sci, Chikusa Ku, Nagoya, Aichi 4648601, Japan

[2] Univ Tokyo, Grad Sch Sci, Bunkyo Ku, Tokyo 1130033, Japan

[3] Kanagawa Univ, Dept Biol Sci, Kanagawa 2591293, Japan

来源：

FEBS LETTERS | 2008年 / 582卷 / 09期

基金：

日本学术振兴会;

关键词：

bacteriochlorophyll biosynthesis; protochlorophyllide reductase; BchN; BchB; nitrogenase MoFe protein; Rhodobacter capsulatus;

D O I：

10.1016/j.febslet.2008.03.018

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1346 / 1350

页数：5

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