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Arabidopsis FNRL protein is an NADPH-dependent chloroplast oxidoreductase resembling bacterial ferredoxin-NADP+ reductases.

Physiol Plant. 2018 Feb;162(2):177-190. doi:10.1111/ppl.12621. Epub 2017 Nov 12
Minna M Koskela 1 , Käthe M Dahlström 2 , Guillermina Goñi 3 , Nina Lehtimäki 1 , Markus Nurmi 1 , Adrian Velazquez-Campoy 4 , Guy Hanke 5 , Bettina Bölter 6 , Tiina A Salminen 2 , Milagros Medina 3 , Paula Mulo 1
Minna M Koskela 1 , Käthe M Dahlström 2 , Guillermina Goñi 3 , Nina Lehtimäki 1 , Markus Nurmi 1 , Adrian Velazquez-Campoy 4 , Guy Hanke 5 , Bettina Bölter 6 , Tiina A Salminen 2 , Milagros Medina 3 , Paula Mulo 1
+ et al

[No authors listed]

Author information
  • 1 Molecular Plant Biology, Department of Biochemistry, University of Turku, Turku, Finland.
  • 2 Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland.
  • 3 Department of Biochemistry and Molecular and Cellular Biology, Faculty of Sciences and Institute of Biocomputation and Physics of Complex Systems (BIFI-IQFR and GBsC-CSIC Joint Units), University of Zaragoza, Zaragoza, Spain.
  • 4 Fundación ARAID, Diputación General de Aragón, Zaragoza, Spain.
  • 5 School of Biochemistry and Chemistry, Queen Mary University of London, London, United Kingdom.
  • 6 Department of Biology I, Botany, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.

摘要


Plastidic ferredoxin-NADP+ oxidoreductases (FNRs; EC:1.18.1.2) together with bacterial type FNRs (FPRs) form the plant-type FNR family. Members of this group contain a two-domain scaffold that forms the basis of an extended superfamily of flavin adenine dinucleotide (FAD) dependent oxidoreductases. In this study, we show that the Arabidopsis thaliana At1g15140 [Ferredoxin-NADP+ oxidoreductase-like (FNRL)] is an FAD-containing NADPH dependent oxidoreductase present in the chloroplast stroma. Determination of the kinetic parameters using the DCPIP NADPH-dependent diaphorase assay revealed that the reaction catalysed by a recombinant FNRL protein followed a saturation Michaelis-Menten profile on the NADPH concentration with kcat  = 3.2 ± 0.2 s-1 , KmNADPH  = 1.6 ± 0.3 μM and kcat /KmNADPH  = 2.0 ± 0.4 μM-1  s-1 . Biochemical assays suggested that FNRL is not likely to interact with Arabidopsis ferredoxin 1, which is supported by the sequence analysis implying that the known Fd-binding residues in plastidic FNRs differ from those of FNRL. In addition, based on structural modelling FNRL has an FAD-binding N-terminal domain built from a six-stranded β-sheet and one α-helix, and a C-terminal NADP+ -binding α/β domain with a five-stranded β-sheet with a pair of α-helices on each side. The FAD-binding site is highly hydrophobic and predicted to bind FAD in a bent conformation typically seen in bacterial FPRs.