Light-Dependent Protochlorophyllide Oxidoreductase: Phylogeny, Regulation, and Catalytic Properties

被引:101
作者
Gabruk, Michal [1 ]
Mysliwa-Kurdziel, Beata [1 ]
机构
[1] Jagiellonian Univ, Fac Biochem Biophys & Biotechnol, Dept Plant Physiol & Biochem, PL-30387 Krakow, Poland
关键词
PROLAMELLAR BODY FORMATION; CHLOROPHYLL BIOSYNTHESIS; TETRAPYRROLE BIOSYNTHESIS; PLASTID IMPORT; NADPH/PROTOCHLOROPHYLLIDE OXIDOREDUCTASE; CRYSTAL-STRUCTURE; ARABIDOPSIS; BODIES; NADPH; IDENTIFICATION;
D O I
10.1021/acs.biochem.5b00704
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
This Current Topic focuses on light-dependent protochlorophyllide oxidoreductase (POR, EC 1.3.1.33). POR catalyzes the penultimate reaction of chlorophyll biosynthesis, i.e., the light-triggered reduction of protochlorophyllide to chlorophyllide. In this reaction, the chlorin ring of the chlorophyll molecule is formed, which is crucial for photosynthesis. POR one of very few enzymes that are driven by light; however, it is unique in the need for its substrate to absorb photons to induce the conformational changes in the enzyme, which are required for its catalytic activation. Moreover, the enzyme is also involved in the negative feedback of the chlorophyll biosynthesis pathway and controls chlorophyll content via its light-dependent activity. Even though it has been almost 70 years since the first isolation of active POR complexes, our knowledge of them has markedly advanced in recent years. In this review, we summarize the current state of knowledge of POP., including the phylogenetic roots of POR, the mechanisms of the regulation of POR genes expression, the regulation of POR activity, the import of POR into plastids, the role of POR in PLB formation, and the molecular mechanism of protochlorophyllide reduction by POR. To the best of our knowledge, no previous review has compiled such a broad set of recent findings about POR.
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页码:5255 / 5262
页数:8
相关论文
共 95 条
[1]   Arabidopsis CAM7 and HY5 Physically Interact and Directly Bind to the HY5 Promoter to Regulate Its Expression and Thereby Promote Photomorphogenesis [J].
Abbas, Nazia ;
Maurya, Jay P. ;
Senapati, Dhirodatta ;
Gangappa, Sreeramaiah N. ;
Chattopadhyay, Sudip .
PLANT CELL, 2014, 26 (03) :1036-1052
[2]   Does a light-harvesting protochlorophyllide alb-binding protein complex exist? [J].
Armstrong, GA ;
Apel, K ;
Rüdiger, WH .
TRENDS IN PLANT SCIENCE, 2000, 5 (01) :40-44
[3]   Greening in the dark: light-independent chlorophyll biosynthesis from anoxygenic photosynthetic bacteria to gymnosperms [J].
Armstrong, GA .
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY, 1998, 43 (02) :87-100
[4]   Monogalactosyldiacylglycerol deficiency in Arabidopsis affects pigment composition in the prolamellar body and impairs thylakoid membrane energization and photoprotection in leaves [J].
Aronsson, Henrik ;
Schottler, Mark A. ;
Kelly, Amelie A. ;
Sundqvist, Christer ;
Dormann, Peter ;
Karim, Sazzad ;
Jarvis, Paul .
PLANT PHYSIOLOGY, 2008, 148 (01) :580-592
[5]  
Bjorn L.O., 2015, PHOTOBIOLOGY, P139
[6]   Comment on "Catalytic Efficiency of a PhotoenzymeAn Adaptation to Natural Light Conditions" by J. Popp et al. [J].
Bjorn, Lars Olof .
CHEMPHYSCHEM, 2013, 14 (11) :2595-2597
[7]   Proteomic analysis of highly purified prolamellar bodies reveals their significance in chloroplast development [J].
Blomqvist, Lisa A. ;
Ryberg, Margareta ;
Sundqvist, Christer .
PHOTOSYNTHESIS RESEARCH, 2008, 96 (01) :37-50
[8]  
Brocker M. J., 2012, HDB PORPHYRIN SCI
[9]   Crystal Structure of the Nitrogenase-like Dark Operative Protochlorophyllide Oxidoreductase Catalytic Complex (ChlN/ChlB)2 [J].
Broecker, Markus J. ;
Schomburg, Sebastian ;
Heinz, Dirk W. ;
Jahn, Dieter ;
Schubert, Wolf-Dieter ;
Moser, Juergen .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2010, 285 (35) :27336-27345
[10]   Regulation and function of tetrapyrrole biosynthesis in plants and algae [J].
Brzezowski, Pawel ;
Richter, Andreas S. ;
Grimm, Bernhard .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2015, 1847 (09) :968-985