Redox regulation of chlorophyll biosynthesis

被引:104
作者
Stenbaek, Anne [1 ]
Jensen, Poul Erik [1 ]
机构
[1] Univ Copenhagen, Fac Life Sci, Dept Plant Biol & Biotechnol, VKR Res Ctr Proact Plants,Mol Plant Biol Lab, DK-1871 Frederiksberg C, Denmark
关键词
Magnesium and ferro chelatase; Mg-protoporphyrin IX methyltransferase; Mg-protoporphyrin monomethyl ester cyclase; NADPH-dependent thioredoxin reductase; Redox; PROTOPORPHYRIN-IX METHYLTRANSFERASE; THIOREDOXIN REDUCTASE; MAGNESIUM CHELATASE; TETRAPYRROLE BIOSYNTHESIS; MG-CHELATASE; 2-CYS PEROXIREDOXINS; CHLOROPLAST DEVELOPMENT; ARABIDOPSIS-THALIANA; NEGATIVE REGULATOR; OXIDATIVE STRESS;
D O I
10.1016/j.phytochem.2010.03.022
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
Chlorophyll captures and redirects light-energy and is thus essential for photosynthetic organisms. The demand for chlorophyll differs throughout the day and night and in response to changing light conditions. Moreover, the chlorophyll biosynthesis pathway is up to certain points shared between the different tetrapyrroles: chlorophyll, heme, siroheme and phytochromobilin, for which the cell has different requirements at different time points. Combined with the phototoxic properties of tetrapyrroles which, if not properly protected, can lead to formation of reactive oxygen species (ROS), the need for a strict regulation of the chlorophyll biosynthetic pathway is obvious. Here we describe the current knowledge on regulation of chlorophyll biosynthesis in plants by the chloroplast redox state with emphasis on the Mg-chelatase situated at the branch point between the heme and the chlorophyll pathway. We discuss the proposed role of the Mg-chelatase as a key regulator of the tetrapyrrole pathway by its effect on enzymes both up- and downstream in the pathway and we specifically describe how redox state might regulate the Mg-branch. Finally, we propose that a recently identified NADPH-dependent thioredoxin reductase (NTRC) could be involved in redox regulation or protection of chlorophyll biosynthetic enzymes and describe the possible modes of action by this enzyme. (C) 2010 Elsevier Ltd. All rights reserved.
引用
收藏
页码:853 / 859
页数:7
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