Nitrogenase Fe protein-like Fe-S cluster is conserved in L-protein (BchL) of dark-operative protochlorophyllide reductase from Rhodobacter capsulatus

被引:43
作者
Nomata, Jiro
Kitashima, Masaharu
Inoue, Kazuhito
Fujita, Yuichi [1 ]
机构
[1] Nagoya Univ, Grad Sch Bioagr Sci, Nagoya, Aichi 4648601, Japan
[2] Kanagawa Univ, Dept Biol Sci, Kanagawa 2591293, Japan
关键词
protochlorophyllide reductase; nitrogenase; bacteriochlorophyll biosynthesis; BchL; Fe-S cluster; Rhodobacter capsulatus; AZOTOBACTER-CHROOCOCCUM; BACTERIOCHLOROPHYLL BIOSYNTHESIS; COMPONENT PROTEINS; IN-VITRO; PURIFICATION; RECONSTITUTION; FERREDOXINS; FIXATION; ENZYME;
D O I
10.1016/j.febslet.2006.10.014
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 reductase (DPOR) in bacteriochlorophyll biosynthesis is a nitrogenase-like enzyme consisting of L-protein (BchL-dimer) as a reductase component and NB-protein (BchN-BchB-heterotetramer) as a catalytic component. Metallocenters of DPOR have not been identified. Here we report that L-protein has an oxygen-sensitive [4Fe-4S] cluster similar to nitrogenase Fe protein. Purified L-protein from Rhodobacter capsulatus showed absorption spectra and an electron paramagnetic resonance signal indicative of a [4Fe-4S] cluster. The activity quickly disappeared upon exposure to air with a half-life of 20 s. These results suggest that the electron transfer mechanism is conserved in nitrogenase Fe protein and DPOR L-protein. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:6151 / 6154
页数:4
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