Brusamarello-Santos, L.C., Gilard, F., Brulé, L., Quilleré, I., Gourion, B., & Ratet, P., et al. (2017). Metabolic profiling of two maize (*Zea mays* L.) inbred lines inoculated with the nitrogen fixing plant-interacting bacteria *Herbaspirillum seropedicae* and *Azospirillum brasilense*. *PLoS One*, 12(3), e0174576.

Buchanan, B.B. (1980). Role of light in the regulation of chloroplast enzymes. *Annual Review of Plant Physiology*, 31, 341–374.

Buchanan, B.B., Schürmann, P., & Kalberer, P.P. (1971). Ferredoxin-activated fructose diphosphatase of spinach chloroplasts. Resolution of the system, properties of the alkaline fructose diphosphatase component, and physiological significance of the ferredoxin-linked activation. *The Journal of Biological Chemistry*, 246, 5952–5959.

Bulen, W.A. (1956). The isolation and characterization of glutamic dehydrogenase from corn leaves. *Archives of Biochemistry and Biophysics*, 62, 173–183.

Caputo, C., Victoria Criado, M., Roberts, I.N., Geslo, M.A., & Barneix, A.J. (2009). Regulation of glutamine synthetase 1 and amino acid transport in the phloem of young wheat plants. *Plant Physiology and Biochemistry*, 47, 335–342.

Carvalho, H., Pereira, S., Sunkel, C., & Salema, R. (1992). Detection of a cytosolic glutamine synthetase in leaves of *Nicotiana tabacum* L. by immunocytochemical methods. *Plant Physiology*, 100, 1591–1594.

Champigny, M.-L., & Bismuth, E. (1976). Role of photosynthetic electron transfer in light activation of Calvin cycle enzymes. *Physiologia Plantarum*, 36, 95–100.

Chardonnet, S., Sakr, S., Cassier-Chauvat, C., Le Maréchal, P., Chauvat, F., & Lemaire, S.D., et al. (2015). First proteomic study of S-glutathionylation in cyanobacteria. *Journal of Proteome Research*, 2, 59–71.

Chen, R.D., Bismuth, E., Champigny, M.L., & Gadal, P. (1989). Chromatographic and immunological evidence that chloroplastic and cytosolic pea leaf NADP-isocitrate dehydrogenases are distinct isoenzymes. *Planta*, 178, 157–163.

Chen, R.D., Bismuth, E., Issakidis, E., Pacot, C., Champigny, M.L., & Gadal, P. (1989). Comparative immunochemistry of NADP-isocitrate dehydrogenase: A highly conserved cytosolic enzyme in higher plants. *Comptes Rendus de l'Académie des Sciences*, 308, 459–465.

Chiadmi, M., Navaza, A., Miginiac-Maslow, M., Jacquot, J.P., & Cherfils, J. (1999). Redox signalling in the chloroplast: Structure of oxidized pea fructose-1,6-bisphosphatase. *EMBO Journal*, 18, 6809–6815.

Chollet, R., Vidal, J., & O'Leary, M.H. (1996). Phosphoenolpyruvate carboxylase: A ubiquitous, highly regulated enzyme in plants. *Annual Review of Plant Physiology and Plant Molecular Biology*, 47, 273–298.

Collin, V., Issakidis-Bourguet, E., Marchand, C., Hirasawa, M., Lancelin, J.-M., & Knaff, D.B., et al. (2003). The Arabidopsis plastidial thioredoxins: New functions and new insights into specificity. *The Journal of Biological Chemistry*, 278, 23747–23752.

Collin, V., Lamkemeyer, P., Miginiac-Maslow, M., Hirasawa, M., Knaff, D.B., & Dietz, K.-J., et al. (2004). Characterization of plastidial thioredoxins from Arabidopsis belonging to the new y-type. *Plant Physiology*, 136, 4088–4095.

Coschigano, K.T., Melo-Oliveira, R., Lim, J., & Coruzzi, G.M. (1998). Arabidopsis *gls* mutants and distinct Fd-GOGAT genes: Implications for photorespiration and primary nitrogen metabolism. *The Plant Cell*, 10, 741–752.

Crawford, N.M., & Arst, N.H., Jr. (1993). The molecular genetics of nitrate assimilation in fungi and Plants. *Annual Review of Genetics*, 27, 115–146.

Crawford, N.A., Droux, M., Kosower, N.S., & Buchanan, B.B. (1989). Evidence for function of the ferredoxin thioredoxin system in the reductive activation of target enzymes of isolated intact chloroplasts. *Archives of Biochemistry and Biophysics*, 271, 223–239.
Cren, M., & Hirel, B. (1999). Glutamine synthetase in higher plants: Regulation of gene and protein expression from the organ to the cell. Plant Cell Physiology, 40, 1187–1193.

Crétin, C., Luchetta, P., Joly, C., Decottignies, P., Lepiniec, L., & Gadal, P., et al. (1990). Primary structure of sorghum malate dehydrogenase (NADP) deduced from cDNA sequence. Homology with malate dehydrogenase (NAD). European Journal of Biochemistry, 192, 299–303.

Crétin, C., Luchetta, P., Joly, C., Miginiac-Maslow, M., Decottignies, P., & Jacquot, J.-P., et al. (1988). Identification of a cDNA clone for sorghum leaf malate dehydrogenase (NADP). Light-dependent mRNA accumulation. European Journal of Biochemistry, 174, 497–501.

Crozet, P., Navarro, F.J., Willmund, F., Mehrshahi, P., Bakowski, K., & Lauersen, K.J., et al. (2018). Birth of a photosynthetic chassis: A MoClo toolkit enabling synthetic biology in the microalga *Chlamydomonas reinhardtii*. ACS Synthetic Biology, 7, 2074–2086.

Cullimore, J.V., Gebhardt, C., Saarelainen, R., Miflin, B.J., Idler, K.B., & Barker, R.F. (1984). Glutamine synthetase of *Phaseolus vulgaris* L.: Organ-specific expression of a multigene family. Journal of Molecular and Applied Genetics, 2, 589–599.

Dai, S., Saarinen, M., Ramaswamy, S., Meyer, Y., Jacquot, J.P., & Eklund, H. (1996). Crystal structure of *Arabidopsis thaliana* thaliana NADPH dependent thioredoxin reductase at 2.5Å° resolution. Journal of Molecular Biology, 264, 1044–1057.

Dai, S., Schwendtmayer, C., Schürmann, P., Ramaswamy, S., & Eklund, H. (2000). Redox signaling in chloroplasts: Cleavage of disulfides by an iron-sulfur cluster. Science, 287, 655–658.

de Lamotte, F., Pruvost, C., Minard, P., Delsuc, M.A., Miginiac-Maslow, M., & Schmitter, J.M., et al. (1997). Structural and functional roles of a conserved proline residue in the alpha-2 helix of *Escherichia coli* thioredoxin. Protein Engineering, 10, 1425–1432.

de Lamotte-Guéry, F., Miginiac-Maslow, M., Decottignies, P., Stein, M., Minard, P., & Jacquot, J.P. (1991). Mutation a negatively charged amino acid in of thioredoxin modifies its reactivity with chloroplastic enzymes. European Journal of Biochemistry, 196, 287–294.

De Silva Conceição, A., & Krebbers, E. (1994). A cotyledon regulatory region is responsible for the different spatial expression patterns of Arabidopsis 2S albumin genes. The Plant Journal, 5, 493–505.

Decottignies, P., Le Maréchal, P., Jacquot, J.P., Schmitter, J.M., & Gadal, P. (1995). Primary structure and post-translational modification of ferredoxin-NADP reductase from *Chlamydomonas reinhardtii*. Archives of Biochemistry and Biophysics, 316, 249–259.

Decottignies, P., Schmitter, J.M., Dutka, S., Jacquot, J.P., & Miginiac-Maslow, M. (1991). Characterization and primary structure of a second thioredoxin from the green alga, *Chlamydomonas reinhardtii*. European Journal of Biochemistry, 198, 505–512.

Decottignies, P., Schmitter, J.M., Jacquot, J.P., Dutka, S., Picaud, A., & Gadal, P. (1990). Purification, characterization and complete amino acid sequence of a thioredoxin from a green alga *Chlamydomonas reinhardtii*. Archives of Biochemistry and Biophysics, 280, 112–121.

Decottignies, P., Schmitter, J.-M., Miginiac-Maslow, M., Le Maréchal, P., Jacquot, J.-P., & Gadal, P. (1988). Primary structure of the light-dependent regulatory site of corn NADP-malate dehydrogenase. The Journal of Biological Chemistry, 263, 11780–11785.

Dellagi, A., Quilleré, I., & Hirel, B. (2020). Beneficial soil borne bacteria and fungi: A promising way to improve plant nitrogen acquisition. Journal of Experimental Botany, 71, 4469–4479. doi:10.1093/jxb/eraa112.

DeWitt, N.D., & Sussman, M.R. (1995). Immunological localization of an epitope-targeged plasma membranes pump (H⁺-ATPase) in phloem companion cells. The Plant Cell, 7, 2053–2076.
Droux, M., Crawford, N.A., & Buchanan, B.B. (1987). Mechanism of thioredoxin-linked activation of chloroplast fructose-1,6-bisphophatase. Comptes Rendus de l'Academie des Sciences. Serie III, Sciences de la Vie, 305, 335-341.

Droux, M., Jacquot, J.-P., Miginiac-Maslow, M., Gadal, P., Huet, J.-C., & Crawford, N.A., et al. (1987). Ferredoxin-thioredoxin reductase, an iron-sulfur enzyme linking light to enzyme regulation in oxygenic photosynthesis: Purification and properties of the enzyme from C3, C4, and cyanobacterial species. Archives of Biochemistry and Biophysics, 252, 426-439.

Droux, M., Miginiac-Maslow, M., Jacquot, J.-P., Gadal, P., Crawford, N.A., & Kosower, N.S., et al. (1987). Ferredoxin-thioredoxin reductase: A catalytically active dithiol group links photoreduced ferredoxin to thioredoxin functional in photosynthetic enzyme regulation. Archives of Biochemistry and Biophysics, 256, 372-380.

Echevarria, C., & Vidal, J. (2003). The unique phosphoenolpyruvate carboxylase kinase. Plant Physiology and Biochemistry, 41, 541-547.

Elliott, W.H. (1953). Isolation of glutamine synthetase and glutamotransferase from green pea. Journal of Biological Chemistry, 201, 661-672.

Feraud, M., Masclaux-Daubresse, C., Ferrario-Méry, S., Pageau, K., Lelandais, M., & Ziegler, C., et al. (2005). Expression of a ferredoxin-dependent glutamate synthase gene in mesophyll and vascular cells and functions of the enzyme in ammonium assimilation in *Nicotiana tabacum* (L.). Planta, 222, 667-677.

Feria Bourrellier, A.B., Ferrario-Méry, S., Vidal, J., & Hodges, M. (2009). Metabolite regulation of the interaction between *Arabidopsis thaliana* PII and N-acetyl-l-glutamate kinase. Biochemical and Biophysical Research Communications, 387, 700-704.

Feria Bourrellier, A.B., Valot, B., Guillot, A., Ambard-Bretteville, F., Vidal, J., & Hodges, M. (2010). Chloroplast acetyl-CoA carboxylase activity is 2-oxoglutarate-regulated by interaction of PII with the biotin carboxyl carrier subunit. Proceedings of the National Academy of Sciences of the United States of America, 107, 502-507.

Fieuw, S., Müller-Röber, B., Gálvez, S., & Willmitzer, L. (1995). Cloning and expression analysis of the cytosolic NADP(+)-dependent isocitrate dehydrogenase from potato. Implications for nitrogen metabolism. Plant Physiology, 107, 905-913.

Fischer, N., Hippler, M., Sétif, M., Jacquot, J.P., & Rochaix, J.D. (1998). The PsaC subunit of photosystem I provides an essential residue for docking of ferredoxin. EMBO Journal, 17, 849-858.

Fontaine, J.X., Tercé-Laforgue, T., Armengaud, P., Clément, G., Renou, J.P., & Pelletier, S., et al. (2012). Characterization of a NADH-dependent glutamate dehydrogenase mutant of Arabidopsis demonstrates the key role of this enzyme in root carbon and nitrogen metabolism. The Plant Cell, 24, 4044-4065.

Gálvez, S., Bismuth, E., Sarda, C., & Gadal, P. (1994). Purification and characterization of chloroplastic NADP-isocitrate dehydrogenase from mixotrophic tobacco cells (comparison with the cytosolic isoenzyme). Plant Physiology, 105, 593-600.

Gálvez, S., Hodges, M., Bismuth, E., Samson, I., Teller, S., & Gadal, P. (1995). Purification and characterization of a fully active recombinant tobacco cytosolic NADP-dependent isocitrate dehydrogenase in *Escherichia coli*: Evidence for a role for the N-terminal region in enzyme activity. Archives of Biochemistry and Biophysics, 323, 164-168.

Gálvez, S., Hodges, M., Decottignies, P., Bismuth, E., Lancien, M., & Sangwan, R.S., et al. (1996). Identification of a tobacco cDNA encoding for a cytosolic NADP-isocitrate dehydrogenase. Plant Molecular Biology, 30, 307-320.

Gálvez, S., Roche, O., Bismuth, E., Brown, S., Gadal, P., & Hodges, M. (1998). Mitochondrial localization of a NADP-dependent isocitrate dehydrogenase isoenzyme by using the green fluorescent protein as a marker.
Gaufichon, L., Marmagne, A., Belcram, K., Yoneyama, T., Sakakibara, Y., & Hase, T., et al. (2017). *ASN1*-encoded asparagine synthetase in floral organs contributes to nitrogen filling in Arabidopsis seeds. The Plant Journal, 91, 371–393.

Gaufichon, L., Masclaux-Daubresse, C., Tcherkez, G., Reisdorf-Cren, M., Sakakibara, Y., & Hase, T., et al. (2013). *Arabidopsis thaliana* *ASN2* encoding asparagine synthetase is involved in the control of nitrogen assimilation and export during vegetative growth. Plant, Cell & Environment, 36, 328–342.

Gaufichon, L., Reisdorf-Cren, M., Rothstein, S.J., Chardon, F., & Suzuki, A. (2010). Biological functions of asparagine synthetase in plants. Plant Science, 179, 141–153.

Gaufichon, L., Rothestein, S., & Suzuki, A. (2016). Asparagine metabolic pathways in Arabidopsis. Plant and Cell Physiology, 57, 675–689.

Goyer, A., Decottignies, P., Issakidis-Bourguet, E., & Miginiac-Maslow, M. (2001). Sites of interaction of thioredoxin with sorghum NADP-malate dehydrogenase. FEBS Letters, 505, 405–408.

Goyer, A., Decottignies, P., Lemaire, S., Ruelland, E., Issakidis-Bourguet, E., & Jacquot, J.-P., et al. (1999). The internal Cys-207 of sorghum leaf NADP-malate dehydrogenase can form mixed disulphides with thioredoxin. FEBS Letters, 444, 165–169.

Goyer, A., Haslekås, C., Miginiac-Maslow, M., Klein, U., Le Maréchal, P., & Jacquot, J.-P., et al. (2002). Isolation and characterization of a thioredoxin-dependent peroxidase from *Chlamydomonas reinhardtii*. European Journal of Biochemistry, 269, 272–282.

Guiz, C., Hirel, B., Schedlofsky, G., & Gadal, P. (1979). Occurrence and influence of light on the relative proportions of two glutamine synthetases in rice leaves. Plant Science Letters, 15, 272–277.

Gütle, D.D., Roret, T., Hecker, A., Reski, R., & Jacquot, J.P. (2017). Dithiol disulphide exchange in redox regulation of chloroplast enzymes in response to evolutionary and structural constraints. Plant Science, 255, 1–11.

Hirasawa, M., Droux, M., Gray, K.A., Boyer, J.M., Davis, D.J., & Buchanan, B.B., et al. (1988). Ferredoxin-thioredoxin reductase: Properties of its complex with ferredoxine. Biochimica et Biophysica Acta, 935, 1–8.

Hirasawa, M., Ruelland, E., Schepens, I., Issakidis-Bourguet, E., Miginiac-Maslow, M., & Knaff, D.B. (2000). Oxidation-reduction properties of the regulatory disulfides of sorghum chloroplast nicotinamide adenine dinucleotide phosphate-malate dehydrogenase. Biochemistry, 39, 3344–3350.

Hirel, B., Bertin, P., Quillere, I., Bourdoncle, W., Attagnant, C., & Dellay, C., et al. (2001). Towards a better understanding of the genetic and physiological basis for nitrogen use efficiency in maize. Plant Physiology, 125, 1258–1270.

Hirel, B., & Gadal, P. (1980a). Glutamine synthetase in rice. A comparative study of the enzymes from roots and leaves. Plant Physiology, 66, 619–623.

Hirel, B., & Gadal, P. (1980b). Sur la localisation intracellulaire de deux formes isofonctionnelles de la glutamine synthétase chez le Riz. Comptes Rendus de l'Académie des Sciences, 291 D, 441–444.

Hirel, B., & Gadal, P. (1981). Glutamine synthetase isoenzymes in pea leaves. Zeitschrift für Pflanzenphysiologie, 102, 315–319.

Hirel, B., & Gadal, P. (1982). Glutamine synthetase isoenzymes in leaves of a C₄ plant: *Sorghum vulgare* L. Physiologia Plantarum, 54, 69–74.

Hirel, B., & Lea, P.J. (2001). Ammonia assimilation. In Lea, P.J., & Morot-Gaudry, J.F. (Eds.), Plant nitrogen (pp. 79–99). Berlin, Heidelberg: Springer.
Hirel, B., Perrot-Rechenmann, C., Suzuki, A., Vidal, J., & Gadal, P. (1982). Glutamine synthetase in spinach leaves. Immunological studies and immuno-cytochemical localization. Plant Physiology, 69, 983-987.

Hoagland, D.R., & Arnon, D.I. (1938). In Circular California Agricultural Experiment Station (Ed.), The water-culture method for growing plants without soil (p. 347). Berkeley, CA: University of California, College of Agriculture, Agricultural Experiment Station.

Hodges, M., Miginiac-Maslow, M., Decottignies, P., Jacquot, J.-P., Stein, M., & Lepiniec, L., et al. (1994). Purification and characterisation of pea thioredoxin f expressed in *Escherichia coli*. Plant Molecular Biology, 26, 225-234.

Holmgren, A., Buchanan, B.B., & Wolosiuk, R.A. (1977). Photosynthetic regulatory protein from rabbit liver is identical with thioredoxin. FEBS Letters, 82, 351-354.

Huppe, H., de Lamotte, F., Jacquot, J.P., & Buchanan, B.B. (1990). The ferredoxin-thioredoxin system of a green alga, Chlamydomonas reinhardtii. Planta, 180, 341-351.

Ireland, R.J., & Lea, P.J. (1999). The enzymes of glutamine, glutamate, asparagine and aspartate metabolism. In Singh, B.K. (Ed.), Plant amino acids (pp. 49-109). New York: Marcel Dekker, Inc.

Issakidis, E., Decottignies, P., & Miginiac-Maslow, M. (1993). A thioredoxin-independent fully active NADP-MDH obtained by site-directed mutagenesis. FEBS Letters, 321, 55-58.

Issakidis, E., Lemaire, M., Decottignies, P., Jacquot, J.-P., & Miginiac-Maslow, M. (1996). Direct evidence for the different roles of the N- and C-terminal regulatory disulfides of sorghum leaf NADP-malate dehydrogenase in its activation by reduced thioredoxin. FEBS Letters, 26, 121-124.

Issakidis, E., Miginiac-Maslow, M., Decottignies, P., Jacquot, J.-P., Crétin, C., & Gadal, P. (1992). Site-directed mutagenesis reveals the involvement of an additional thioredoxin-dependent regulatory site in the activation of recombinant sorghum leaf NADP-malate dehydrogenase. The Journal of Biological Chemistry, 267, 21577-21583.

Issakidis, E., Saarinen, M., Decottignies, P., Jacquot, J.-P., Crétin, C., & Gadal, P., et al. (1994). Identification and characterization of the second regulatory disulfide bridge of recombinant sorghum leaf NADP-malate dehydrogenase. The Journal of Biological Chemistry, 269, 3511-3517.

Issakidis-Bourguet, E., Lavergne, D., Trivelli, X., Decottignies, P., & Miginiac-Maslow, M. (2006). Transferring redox regulation properties from sorghum NADP-malate dehydrogenase to *Thermus* NAD-malate dehydrogenase. Photosynthesis Research, 89, 213-223.

Issakidis-Bourguet, E., Mouaheb, N., Meyer, Y., & Miginiac-Maslow, M. (2001). Heterologous complementation of yeast reveals a new putative function for chloroplast m-type thioredoxin. The Plant Journal, 25, 127-135.

Jacquot, J.P., Buchanan, B.B., Martin, F., & Vidal, J. (1981). Enzyme regulation in C4 photosynthesis: Purification and properties of thioredoxin linked NADP malate dehydrogenase from corn leaves. Plant Physiology, 68, 300-304.

Jacquot, J.P., de Lamotte-Guéry, F., Fontecave, M., Schürmann, P., Decottignies, P., & Miginiac-Maslow, M., et al. (1990). Human thioredoxin reactivity: Structure-function relationship. Biochemical and Biophysical Research Communications, 173, 1375-1381.

Jacquot, J.-P., Droux, M., Miginiac-Maslow, M., Joly, C., & Gadal, P. (1984). Frozen thylakoids—An improvement for reconstituted chloroplast enzyme light-activation systems. Plant Science Letters, 35, 181-185.

Jacquot, J.-P., Keryer, E., Issakidis, E., Decottignies, P., Miginiac-Maslow, M., & Schmitter, J.-M., et al. (1991). Properties of recombinant NADP-malate dehydrogenases from *Sorghum vulgare* leaves expressed in *Escherichia coli* cells. European Journal of Biochemistry, 199, 47-51.
Jacquot, J.P., Lopez-Jaramillo, J., Chueca, A., Cherfils, J., Lemaire, S., & Chedozeau, B., et al. (1995). High level expression of recombinant pea chloroplast fructose-1,6-bisphosphatase and mutagenesis of its regulatory site. European Journal of Biochemistry, 229, 675-681.

Jacquot, J.P., Lopez-Jaramillo, J., Miginiac-Maslow, M., Lemaire, S., Cherfils, J., & Chueca, A., et al. (1997). Cysteine 153 is required for redox regulation of pea chloroplast fructose-1,6-bisphosphatase. FEBS Letters, 401, 143-147.

Jacquot, J.P., Maudinas, B., & Gadal, P. (1979). Occurence of thioredoxins m in the photosynthetic bacteria *Rhodopseudomonas capsulata*. Biochemical and Biophysical Research Communications, 91, 1371-1376.

Jacquot, J.P., Rivera-Madrid, R., Marinho, P., Kollarova, M., Le Maréchal, P., & Miginiac-Maslow, M., et al. (1994). *Arabidopsis thaliana thaliana* NADPH thioredoxin reductase. Journal of Molecular Biology, 235, 1357-1363.

Jacquot, J.P., Stein, M., Hodges, M., & Miginiac-Maslow, M. (1992). PCR cloning of a nucleotidic sequence coding for the mature part of *Chlamydomonas reinhardtii* thioredoxin Ch2. Nucleic Acids Research, 20, 617.

Jacquot, J.P., Stein, M., Suzuki, A., Liottet, S., Sandoz, G., & Miginiac-Maslow, M. (1997). Residue Glu 91 of *Chlamydomonas reinhardtii* ferredoxin is essential for electron transfer to ferredoxin thioredoxin reductase. FEBS Letters, 400, 293-296.

Jacquot, J.P., Vidal, J., & Gadal, P. (1976). Identification of a protein factor involved in dithiothreitol activation of NADP-malate dehydrogenase from French bean leaves. FEBS Letters, 71, 223-227.

Jacquot, J.P., Vidal, J., & Gadal, P. (1977). Evidence for chloroplastic localization of spinach leaf NADP-malate dehydrogenase activating factors. Planta, 137, 89-90.

Jacquot, J.-P., Vidal, J., Gadal, P., & Schürmann, P. (1978). Evidence for the existence of several enzyme-specific thioredoxins in plants. FEBS Letters, 96, 243-246.

James, D., Borphukan, B., Fartyal, D., Achary, V.M.M., & Reddy, M.K. (2018). Transgenic manipulation of glutamine synthetase: a target with untapped potential in various aspects of crop improvement. In Gosal, S.S., & Wani, S.H. (Eds.), Biotechnology of crop improvement (pp. 367-416). Springer International Publishing AG.

Johansson, K., Ramaswamy, S., Saarinen, M., Lemaire-Chamley, M., Issakidis-Bourguet, E., & Miginiac-Maslow, M., et al. (1999). Structural basis for light activation of a chloroplast enzyme: The structure of sorghum NADP-malate dehydrogenase in its oxidized form. Biochemistry, 38, 4319-4326.

Johnson, H.S., & Hatch, M.D. (1970). Properties and regulation of leaf nicotinamide-adenine dinucleotide phosphate-malate dehydrogenase and "malic" enzyme in plants with the C4-dicarboxylic acid pathway of photosynthesis. Biochemical Journal, 119, 273-280.

Joy, K.W., & Hageman, R.H. (1966). The purification and properties of nitrite reductase from higher plants, and its dependence on ferredoxin. Biochemical Journal, 100, 263-273.

Kagawa, T., & Hatch, M.D. (1977). Regulation of C4 photosynthesis—characterization of a protein factor mediating activation and inactivation of NADP-malate dehydrogenase. Archives of Biochemistry and Biophysics, 184, 290-297.

Kamachi, K., Yamaya, T., Hayakawa, T., Mae, T., & Ojima, K. (1992). Vascular bundle-specific localization of cytosolic glutamine synthetase in rice leaves. Plant Physiology, 99, 1481-1486.

Kanamori, T., & Mastumoto, H. (1972). Glutamine synthetase from rice plants. Archives of Biochemistry and Biophysics, 125, 404-412.

Keryer, E., Collin, V., Lavergne, D., Lemaire, S., & Issakidis-Bourguet, E. (2004). Characterization of Arabidopsis mutants for the variable subunit of ferredoxin:thioredoxin reductase. Photosynthesis Research, 79, 265-274.
Keys, A.F., Bird, I.F., Cornelius, M.J., Lea, P.J., Wallsgrove, R.M., & Miflin, B.J. (1978). Photorespiratory nitrogen cycle. Nature, 275, 741–742.

Knaff, D.B., & Hirasawa, M. (1991). Ferredoxin-dependent chloroplast enzymes. Biochimica et Biophysica Acta, 1056, 93–125.

Kobe, B., & Kemp, B.E. (1999). Active site-directed protein regulation. Nature, 402, 373–376.

Krimm, I., Goyer, A., Issakidis-Bourguet, E., Miginiac-Maslow, M., & Lancelin, J.-M. (1999). Direct NMR observation of the thioredoxin-mediated reduction of the chloroplast NADP-malate dehydrogenase provides a structural basis for the relief of autoinhibition. The Journal of Biological Chemistry, 274, 34539–34542.

Labboun, S., Tercé-Laforgue, T., Roscher, A., Bedu, M., Restivo, F.M., & Velanis, C.N., et al. (2009). Resolving the role of plant glutamate dehydrogenase: I. *In vivo* real time nuclear magnetic resonance spectroscopy experiments. Plant Cell Physiology, 50, 1761–1773.

Lam, H.-M., Coschigano, K.T., Oliveira, I.C., Melo-Oliveira, R., & Coruzzi, G.M. (1996). The molecular genetics of nitrogen assimilation into amino acids in higher plants. Annual Review of Plant Physiology and Plant Molecular Biology, 47, 569–593.

Lamkemeyer, P., Laxa, M., Collin, V., Li, W., Finkemeier, I., & Schöttler, M.A., et al. (2006). Peroxiredoxin Q of *Arabidopsis thaliana* is attached to the thylakoids and functions in context of photosynthesis. The Plant Journal, 45, 968–981.

Lancelin, J.M., Bally, I., Arlaud, G.J., Blackledge, M., Gans, P., & Stein, M., et al. (1994). NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution. FEBS Letters, 343, 261–266.

Lancelin, J.M., Stein, M., & Jacquot, J.P. (1993). Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga *Chlamydomonas reinhardtii* as determined by ¹H NMR. Journal of Biochemistry, 114, 421–431.

Lancien, M., Ferrario-Méry, S., Roux, Y., Bismuth, E., Masclaux, C., & Hirel, B., et al. (1999). Simultaneous expression of NAD-dependent isocitrate dehydrogenase and other Krebs cycle genes after nitrate resupply to short-term nitrogen starved *Nicotiana tabacum*. Plant Physiology, 120, 717–725.

Lancien, M., Gadal, P., & Hodges, M. (1998). Molecular characterization of higher plant NAD-dependent isocitrate dehydrogenase: Evidence for a heteromeric structure by the complementation of yeast mutants. Plant Journal, 16, 325–333.

Lara, C., De la Torre, A., & Buchanan, B.B. (1980). Ferralterin: An iron-sulfur protein functional in enzyme regulation in photosynthesis. Biochemical and Biophysical Research Communications, 94, 1337–1344.

Laugier, E., Tarrago, L., Courteille, A., Innocenti, G., Eymery, F., & Rumeau, D., et al. (2013). Involvement of thioredoxin y2 in the preservation of leaf methionine sulfoxide reductase capacity and growth under high light. Plant, Cell & Environment, 36, 670–682.

Lea, P.J., & Miflin, B.J. (1974). Alternative route for nitrogen assimilation in higher plants. Nature, 251, 614–616.

Lea, P.J., & Miflin, B.J. (2018). Nitrogen assimilation and its relevance to crop improvement. In Foyer, C.H., & Zhang, H. (Eds.), Nitrogen metabolism in plants in the post-genomic era: Vol. 42. Annual plant reviews (pp. 1–40). Chichester, UK: Wiley-Blackwell.

Lemaire, S.D., Guillon, B., Le Maréchal, P., Keryer, E., Miginiac-Maslow, M., & Decottignies, P. (2004). New thioredoxin targets in the unicellular photosynthetic eukaryote *Chlamydomonas reinhardtii*. Proceedings of the National Academy of Sciences of the United States of America, 101, 7475–7480.

Lemaire, S.D., Hours, M., Gérard-Hirne, C., Trouabal, A., Roche, O., & Jacquot, J.-P. (1999). Analysis of light/dark synchronization of cell-wall-less *Chlamydomonas reinhardtii* (Chlorophyta) cells by flow cytometry.
European Journal of Phycology, 34, 279-286.

Lemaire, S., Keryer, E., Stein, M., Schepens, I., Issakidis-Bourguet, E., & Gérard-Hirne, C., et al. (1999). Heavy-metal regulation of thioredoxin gene expression in *Chlamydomonas reinhardtii*. *Plant Physiology*, 120, 773-778.

Lemaire, M., Miginiac-Maslow, M., & Decottignies, P. (1996). The catalytic site of chloroplastic NADP-dependent malate dehydrogenase contains a His/Asp pair. *European Journal of Biochemistry*, 236, 947-952.

Lemaire, S.D., Quesada, A., Merchan, F., Corral, J.M., Igeno, M.I., & Keryer, E., et al. (2005). NADP-malate dehydrogenase from unicellular green alga *Chlamydomonas reinhardtii*. A first step toward redox regulation? *Plant Physiology*, 137, 514-521.

Lemaire, S.D., Richardson, J.M., Goyer, A., Keryer, E., Lancelin, J.-M., & Makhatadze, G.I., et al. (2000). Primary structure determinants of the pH- and temperature-dependent aggregation of thioredoxin. *Biochimica et Biophysica Acta*, 1476, 311-323.

Lemaire, M., Schmitter, J.-M., Issakidis, E., Miginiac-Maslow, M., Gadal, P., & Decottignies, P. (1994). Essential histidine at the active site of sorghum leaf NADP-dependent malate dehydrogenase. *The Journal of Biological Chemistry*, 269, 27291-27296.

Lemaitre, T., Urbanczyk-Wochniak, E., Flesch, V., Bismuth, E., Fernie, A.R., & Hodges, M. (2007). NAD-dependent isocitrate dehydrogenase mutants of *Arabidopsis* suggest the enzyme is not limiting for nitrogen assimilation. *Plant Physiology*, 144, 1546-1558.

Lepiniec, L., Thomas, M., & Vidal, J. (2003). From enzyme activity to plant biotechnology: 30 years of research on phosphoenolpyruvate carboxylase. *Plant Physiology* and *Biochemistry*, 41, 533-539.

Lillig, C.H., Prior, A., Schwenn, J.D., Aslund, F., Ritz, D., & Vlamis-Gardikas, A., et al. (1999). New thioredoxins and glutaredoxins as electron donors of 3'-phosphoadenylylsulfate reductase. *The Journal of Biological Chemistry*, 274, 7695-7698.

Lockard, R.G. (1959). In Hewitt, E.J. (Ed.), *Sand and water culture methods* (p. 547). Table 30C Bucks, England: The Commonwealth Agricultural Bureau.

Lopez-Jaramillo, J., Chueca, A., Jacquot, J.P., Hermoso, R., Lazaro, J.J., & Sahrawy, M., et al. (1997). High-yield expression of pea thioredoxin m and assessment of its efficiency in chloroplast fructose-1,6-bisphosphatase activation. *Plant Physiology*, 114, 1169-1175.

Lowry, O.H., Rosenbrowgh, N.J., Farr, A.L., & Randall, R.J. (1951). Protein measurement with folin phenol reagent. *Journal of Biological Chemistry*, 193, 265-275.

Marchand, C., Le Maréchal, P., Meyer, Y., Miginiac-Maslow, M., Issakidis-Bourguet, E., & Decottignies, P. (2004). New targets of Arabidopsis thioredoxins revealed by proteomic analysis. *Proteomics*, 4, 2696-2706.

Marchand, C.H., Vanacker, H., Collin, V., Issakidis-Bourguet, E., Le Maréchal, P., & Decottignies, P. (2010). Thioredoxin targets in Arabidopsis roots. *Proteomics*, 10, 2418-2428.

Martin, A., Lee, J., Kichey, T., Gerentes, D., Zivy, M., & Tatou, C., et al. (2006). Two cytosolic glutamine synthetase isoforms of maize (*Zea mays* L.) are specifically involved in the control of grain production. *The Plant Cell*, 18, 3252-3274.

Masclaux, C., Quilleré, I., Gallais, A., & Hirel, B. (2001). The challenge of remobilisation in plant nitrogen economy. A survey of physio-agronomic and molecular approaches. *Annals of Applied Biology*, 138, 69-81.

Masclaux-Daubresse, C., Reisdorf-Cren, M., Pageau, K., Lelandais, M., Grandjean, O., & Kronenberger, J., et al. (2006). Glutamine synthetase/glutamate synthase pathway and glutamate dehydrogenase play distinct roles for sink/source nitrogen cycle in tobacco (*Nicotiana tabacum* L.). *Plant Physiology*, 140, 444-456.
Maudinas, B., Chemardin, M., Yovanovitch, E., & Gadal, P. (1981). Gnotobiotic cultures of rice plants up to ear stage in the absence of combined nitrogen source but in the presence of free-living nitrogen fixing bacteria *Azotobacter vinelandii* and *Rhodopseudomonas capsulata*. Plant and Soil, 60, 85-97.

McNally, S.F., Hirel, B., Gadal, P., Mann, A.F., & Stewart, G.R. (1983). Glutamine synthetase of higher plants: Evidence for a specific isoenzyme content related to their possible physiological role and their compartmentation within the leaf. Plant Physiology, 72, 22-25.

Miao, G.H., Hirel, B., Marsolier, M.C., Ridge, R.W., & Verma, D.P.S. (1991). Ammonia regulated expression of a soybean gene encoding cytosolic glutamine synthetase in transgenic *Lotus corniculatus*. The Plant Cell, 3, 11-22.

Michelet, L., Zaffagnini, M., Marchand, C., Collin, V., Decottignies, P., & Tsan, P., et al. (2005). Glutathionylation of chloroplast thioredoxin f is a redox signaling mechanism in plants. Proceedings of the National Academy of Sciences of the United States of America, 102, 16478-16483.

Michelet, L., Zaffagnini, M., Morisse, S., Sparla, F., Perez-Perez, M.-E., & Francia, F., et al. (2013). Redox regulation of the Calvin-Benson cycle: Something old, something new. Frontiers in Plant Science, 4, 470.

Miflin, B.J., & Lea, P.J. (1975). Glutamine and asparagine as nitrogen donors for reductant-dependent glutamate synthesis in roots. Biochemical Journal, 149, 403-409.

Miflin, B.J., & Lea, P.J. (1977). Amino acid metabolism. Annual Review of Plant Physiology, 28, 299-329.

Miginiac-Maslow, M., Decottignies, P., Jacquot, J.-P., & Gadal, P. (1990). Regulation of corn leaf NADP-malate dehydrogenase light-activation by the photosynthetic electron flow. Effect of photoinhibition studied in a reconstituted system. Biochimica et Biophysica Acta, 1017, 273-279.

Miginiac-Maslow, M., & Hoarau, A. (1975). The reducing power and the CO₂ fixation activity of isolated choroplasts. Physiologia Plantarum, 35, 186-190.

Miginiac-Maslow, M., Jacquot, J.-P., & Droux, M. (1985). Energetic aspects of the light activation of two chloroplast enzymes: Fructose-1,6-bisphosphatase and NADP-malate dehydrogenase. Photosynthesis Research, 6, 201-213.

Mittard, V., Morelle, N., Brutscher, B., Simorre, J.P., Marion, D., & Stein, M., et al. (1995). 1H, 13C, 15N-NMR resonance assignments of oxidized thioredoxin h from the eukaryotic green alga *Chlamydomonas reinhardtii* using new methods based on two-dimensional triple resonance NMR spectroscopy and computer assisted backbone assignment. European Journal of Biochemistry, 229, 473-485.

Morisse, S., Zaffagnini, M., Gao, X.H., Lemaire, S.D., & Marchand, C.H. (2014). Insight into protein S-nitrosylation in *Chlamydomonas reinhardtii*. Antioxidants & Redox Signaling, 20, 1271-1284.

Oaks, A. (1995). Evidence for deamination by glutamate dehydrogenase in higher plants: Reply. Canadian Journal of Botany, 73, 1116-1117.

Oliver, G., Gosset, G., Sanchez-Pescador, R., Lozoya, E., Ku, L.M., & Flores, N., et al. (1987). Determination of the nucleotide sequence for the glutamate synthase structural genes of *Escherichia coli* K-12. Gene, 60, 1-11.

Plett, D., Garnett, T.P., & Okamoto, M. (2017). Molecular genetics to discover and improve nitrogen use efficiency in crop plants. In Anwar Hossain, M., Kamiya, T., Buritt, D., Phan Tran, L.S., & Fujiwara, T. (Eds.), Plant macronutrient use efficiency (pp. 93-122). Academic Press.

Potel, F., Valadier, M.-H., Ferrario-Méry, S., Grandjean, O., Marin, H., & Gaufichon, L., et al. (2009). Assimilation of excess ammonium into amino acids and nitrogen translocation in Arabidopsis thaliana—Roles of glutamate synthases and carbamoylphosphate synthetase in leaves. The FEBS Journal, 276, 4061-4076.

Rahantaniaina, M.-S., Li, S., Chatel-Innocenti, G., Tuzet, A., Issakidis-Bourguet, E., & Mhamdi, A., et al. (2017). Cytosolic and chloroplastic DHARs cooperate in oxidative stress-driven activation of the salicylic acid pathway. Plant Physiology, 174, 956-971.
Rivera-Madrid, R., Mestres, D., Marinho, P., Jacquot, J.P., Decottignies, P., & Miginiac-Maslow, M., et al. (1995). Evidence for five divergent thioredoxin h sequences in *Arabidopsis thaliana*. Proceedings of the National Academy of Sciences of the United States of America, 92, 5620–5624.

Rogers, W.J., Hodges, M., Decottignies, P., Schmitter, J.-M., Gadal, P., & Jacquot, J.-P. (1992). Isolation of a cDNA fragment coding for *Chlamydomonas reinhardtii* ferredoxin and expression of the recombinant protein in *Escherichia coli*. FEBS Letters, 310, 240–245.

Ruelland, E., Johansson, K., Decottignies, P., Djukic, N., & Miginiac-Maslow, M. (1998). The autoinhibition of sorghum NADP malate dehydrogenase is mediated by a C-terminal negative charge. The Journal of Biological Chemistry, 273, 33482–33488.

Ruelland, E., Lemaire-Chamley, M., Le Maréchal, P., Issakidis-Bourguet, E., Djukic, N., & Miginiac-Maslow, M. (1997). An internal cysteine is involved in the thioredoxin-dependent activation of sorghum leaf NADP-malate dehydrogenase. The Journal of Biological Chemistry, 272, 19851–19857.

Sanger, F., Nicklen, S., & Coulson, A.R. (1977). DNA sequencing with chain-terminating inhibitors. Proceedings of the National Academy of Sciences of the United States of America, 74, 5463–5467.

Scheibe, R. (2004). Malate valves to balance cellular energy supply. Physiologia Plantarum, 120, 24–29.

Scheibe, R., & Jacquot, J.-P. (1983). NADP regulates the light activation of NADP-dependent malate dehydrogenase. Planta, 157, 548–553.

Schepens, I., Decottignies, P., Ruelland, E., Johansson, K., & Miginiac-Maslow, M. (2000). The dimer contact area of sorghum NADP-malate dehydrogenase: Role of aspartate 101 in dimer stability and catalytic activity. FEBS Letters, 471, 240–244.

Schepens, I., Johansson, K., Decottignies, P., Gillibert, M., Hirasawa, M., & Knaff, D.B., et al. (2000). Inhibition of the thioredoxin-dependent activation of the NADP-malate dehydrogenase and cofactor specificity. The Journal of Biological Chemistry, 275, 20996–21001.

Schepens, I., Ruelland, E., Miginiac-Maslow, M., Le Maréchal, P., & Decottignies, P. (2000). The role of active site arginines of sorghum NADP-malate dehydrogenase in thioredoxin-dependent activation and activity. The Journal of Biological Chemistry, 275, 35792–35798.

Schmitter, J.M., Jacquot, J.P., de Lamotte-Guéry, F., Beauvallet, C., Dutka, S., & Gadal, P., et al. (1988). Purification, properties and complete amino-acid sequence of the ferredoxin from a green alga, *Chlamydomonas reinhardtii*. European Journal of Biochemistry, 172, 405–412.

Schröder, M., Giermann, N., & Zrenner, R. (2005). Functional analysis of the pyrimidine de novo synthesis pathway in *Solanaceous* species. Plant Physiology, 138, 1926–1938.

Schürmann, P., & Jacquot, J.P. (1979). Improved in vitro light activation and assay systems for two spinach chloroplast enzymes. Biochimica et Biophysica Acta, 569, 309–312.

Schürmann, P., Wolosiuk, R.A., Breazeale, V.D., & Buchanan, B.B. (1976). Two proteins function in the regulation of photosynthetic CO2 assimilation in chloroplasts. Nature, 263, 257–258.

Scopes, R.K. (1974). Measurement of protein by spectrophotometry at 205 nm. Analytical Biochemistry, 59, 277–282.

Shin, M., & Oshino, R.J. (1978). Ferredoxin-sepharose 4B as a tool for the purification of ferredoxin-NADP reductase. Biochemical Journal, 83, 357–361.

Skopelitis, D., Paranychiankis, N.V., Paschalidis, K.A., Plianokis, E.D., Delis, I.D., & Yakoumakis, D., et al. (2006). Abiotic stress generates ROS that signal expression of anionic glutamate dehydrogenase to form glutamate for proline synthesis in tobacco and grapevine. Plant Cell, 18, 2767–2781.
Smith, E.L., Austen, B.M., Blumenthal, K.M., & Nyc, J.F. (1975). 5 Glutamate dehydrogenases. The Enzymes, 11, 293–367.

Somerville, C.R., & Ogren, W.L. (1980). Inhibition of photosynthesis in Arabidopsis mutants lacking in leaf glutamate synthase activity. Nature, 286, 257–259.

Stein, M., Chedozeau, B., & Jacquot, J.P. (1996). Cloning and sequencing of a ferredoxin gene (Genbank U29516) from *Chlamydomonas reinhardtii*. Plant Physiology, 109, 721.

Stein, M., Jacquot, J.P., Jeannette, E., Decottignies, P., Hodges, M., & Lancelin, J., et al. (1995). *Chlamydomonas reinhardtii* thioredoxins: Structure of the genes coding for the chloroplastic m and cytosolic h isoforms; expression in Escherichia coli of the recombinant proteins, purification and biochemical properties. Plant Molecular Biology, 28, 487–503.

Stein, M., Jacquot, J.P., & Miginiac-Maslow, M. (1993). A cDNA clone encoding *Chlamydomonas reinhardtii* preferredoxin. Plant Physiology, 102, 1349–1350.

Stewart, G.R., Shatilov, V.R., Turnbull, M.H., Robinson, S.A., & Goodall, R. (1995). Evidence that glutamate dehydrogenase plays a role in oxidative deamination of glutamate in seedlings of *Zea mays*. Australian Journal of Plant Physiology, 22, 805–809.

Suzuki, A., Audet, C., & Oaks, A. (1987). Influence of light on the ferredoxin-dependent glutamate synthase in maize leaves. Plant Physiology, 84, 578–581.

Suzuki, A., Burkhart, W., & Rothstein, S. (1996). Nitrogen effects on the induction of ferredoxin-dependent glutamate synthase and its mRNA in maize leaves under the light. Plant Science, 114, 83–91.

Suzuki, A., & Gadal, P. (1982). Glutamate synthase from rice leaves. Plant Physiology, 69, 848–852.

Suzuki, A., & Gadal, P. (1984). Glutamate synthase. Physicochemical and functional properties of different forms in higher plants and in other organisms. Physiologie Végétale, 22, 471–486.

Suzuki, A., Gadal, P., & Oaks, A. (1981). Intracellular distribution of enzymes associated with nitrogen assimilation in roots. Planta, 151, 457–461.

Suzuki, A., Jacquot, J.P., & Gadal, P. (1983). Glutamate synthase in rice roots. Studies on the electron donor specificity. Phytochemistry, 22, 1543–1546.

Suzuki, A., & Knaff, D.B. (2005). Glutamate synthase: Structural, mechanistic and regulatory properties, and role in the amino acid metabolism. Review. Photosynthesis Research, 83, 191–217.

Suzuki, A., Oaks, A., Jacquot, J.P., Vidal, J., & Gadal, P. (1985). An electron donor system in maize roots for reaction of glutamate synthase and nitrite reductase. Physiological and immunological properties of the electron carrier and pyridine nucleotide reductase. Plant Physiology, 78, 374–378.

Suzuki, A., Rioual, S., Lemarchand, S., Godfroy, N., Roux, Y., & Boutin, J.P., et al. (2001). Regulation by light and metabolite of ferredoxin-dependent glutamate synthase in maize. Physiologia Plantarum, 112, 524–530.

Suzuki, A., & Rothstein, S. (1997). Structure and regulation of ferredoxin-dependent glutamate synthase in *Arabidopsis thaliana*. Cloning of cDNA, expression of different tissues of wild-type and *gltS* mutant strains, and light induction. European Journal of Biochemistry, 243, 708–718.

Suzuki, A., Vergnet, C., Morot-Gaudry, J.-F., Zehnacker, C., & Grosclaude, J. (1994). Immunological characterization of ferredoxin and methyl viologen interacting domains of glutamate synthase using monoclonal antibodies. Plant Physiology and Biochemistry, 32, 619–626.

Suzuki, A., Vidal, J., & Gadal, P. (1982). Glutamate synthase isoforms. Immunological studies of enzymes in green leaf, etiolated leaf and root tissues. Plant Physiology, 70, 827–832.
Suzuki, A., Vidal, J., Nguyen, J., & Gadal, P. (1984). Occurrence of ferredoxin-dependent glutamate synthase in plant cell fraction of soybean nodules (*Glycine max*). FEBS Letters, 173, 204–208.

Thomsen, H.C., Eriksson, D., Moller, I.S., & Schojoerring, J.K. (2014). Cytosolic glutamine synthetase: A target for improvement of crop nitrogen use efficiency? Trends in Plant Science, 19, 656–663.

Thormählen, I., Ruber, J., von Roepenack-Lahaye, E., Ehrlich, S.M., Massot, V., & Hümmer, C., et al. (2013). Inactivation of thioredoxin f1 leads to decreased light activation of ADP-glucose pyrophosphorylase and altered diurnal starch turnover in leaves of Arabidopsis plants. Plant, Cell & Environment, 36, 16–29.

Thormählen, I., Zupok, A., Rescher, J., Leger, J., Weissenberger, S., & Groysman, J., et al. (2017). Thioredoxins play a crucial role in dynamic acclimation of photosynthesis in fluctuating light. Molecular Plant, 10, 168–182.

Truernit, E., Bauby, H., Dubreucq, B., Grandjean, O., Runions, J., & Barathélémy, J., et al. (2008). High-resolution whole-mount imaging of three-dimensional tissue organisation and gene expression enables the study of phloem development and structure in Arabidopsis. The Plant Cell, 20, 1494–1503.

Valadier, M.-H., Yoshida, A., Grandjean, O., Morin, H., Kronenberger, J., & Boutet, S., et al. (2008). Implication of the glutamine synthetase-glutamate synthase pathway in conditioning the amino acid metabolism in bundle sheath and mesophyll cells of maize leaves. FEBS Journal, 275, 3193–3206.

Vanacker, H., Guichard, M., Bohrer, A.-S., & Issakidis-Bourguet, E. (2018). Redox regulation of monodehydroascorbate reductase by thioredoxin y in plastids revealed in the context of water stress. Antioxidants, 7, E183.

Vavitsas, K., Crozet, P., Vinde, M.H., Davies, F., Lemaire, S.D., & Vickers, C.E. (2019). The synthetic biology toolkit for photosynthetic microorganisms. Plant Physiology, 181, 14–27.

Vidal, J., Cavalie, G., & Gadal, P. (1976). Studies on bean and sorghum phosphoenolpyruvate carboxylase with polyacrylamide gel electrophoresis. Plant Science Letters, 7, 265–270.

Vidal, J., & Chollet, R. (1997). Regulatory phosphorylation of C₄ PEPC carboxylase. Trends in Plant Science, 2, 230–237.

Vidal, J., Jacquot, J.P., & Gadal, P. (1980). Light activation of NADP malate dehydrogenase in a reconstituted chloroplastic system. Phytochemistry, 19, 1919–1924.

Vidal, J., Jacquot, J.P., Gadal, P., & Vidal, D. (1978). Influence of protein factors on activation of NADP-malate dehydrogenase by dithiothreitol. Physiologia Plantarum, 42, 307–314.

Vidal, J., Jacquot, J.P., Membre, H., & Gadal, P. (1978). Detection and study of protein factors involved in dithiothreitol activation of NADP-malate dehydrogenase from a C4 plant. Plant Science Letters, 11, 305–310.

Wallsgrove, R.M., Turner, J.C., Hall, N.P., Kendall, A.C., & Bright, S.W.J. (1987). Barley mutants lacking chloroplast glutamine synthetase. Biochemical and genetic analysis. Plant Physiology, 83, 155–158.

Walters, E.M., Garcia-Serres, R., Jameson, G.N., Glauser, D.A., Bourquin, F., & Manieri, W., et al. (2005). Spectroscopic characterization of site-specific [Fe(4)S(4)] cluster chemistry in ferredoxin:thioredoxin reductase: Implications for the catalytic mechanism. Journal of the American Chemical Society, 127, 9612–9624.

Wetterauer, B., Jacquot, J.P., & Véron, M. (1992). Thioredoxins from *Dictyostelium discoideum* are a developmentally regulated multigene family. The Journal of Biological Chemistry, 267, 9895–9904.

Wildner, G.F., & Criddle, R.S. (1969). Ribulose diphosphate carboxylase I. A factor involved in light activation of the enzyme. Biochemical and Biophysical Research Communications, 37, 952–956.

Wollmann, E., d'Auriol, L., Rimsky, L., Shaw, A., Jacquot, J.P., & Wingfield, P., et al. (1988). Cloning and expression of a cDNA for human thioredoxin. The Journal of Biological Chemistry, 263, 15506–15512.
Wolosiuk, R.A., & Buchanan, B.B. (1977). Thioredoxin and glutathione regulate photosynthesis in chloroplasts. *Nature*, 266, 565-567.

Wolosiuk, R.A., Buchanan, B.B., & Crawford, N.A. (1977). Regulation of NADP-malate dehydrogenase by the light-activated ferredoxin/thioredoxin system of chloroplasts. *FEBS Letters*, 81, 253-258.

Wolosiuk, R.A., Crawford, N.A., & Buchanan, B.B. (1979). Isolation of three thioredoxins from spinach leaves. *The Journal of Biological Chemistry*, 254, 1627-1632.

Yoneyama, T., & Suzuki, A. (2019). Exploration of nitrate-to-glutamate assimilation in non-photosynthetic roots of higher plants by studies of ¹⁵N-tracing, enzymes involved, reductant supply, and nitrate signaling: A review and synthesis. *Plant Physiology and Biochemistry*, 136, 245-254.

Zaffagnini, M., Bedhomme, M., Groni, H., Marchand, C.H., Puppo, C., & Gontero, B., et al. (2012). Glutathionylation in the photosynthetic model organism *Chlamydomonas reinhardtii*: a proteomic survey. *Molecular and Cellular Proteomics*, 11, M111.014142.

Q28

Ziegler, C., Feraud, M., Jouglet, T., Viret, L., Spampinato, A., & Paganelli, V., et al. (2003). Regulation of promoter activity of ferredoxin-dependent glutamate synthase. *Plant Physiology and Biochemistry*, 41, 649-655.

Picault, N., Palmieri, L., Pisano, M., & Palmieri, F. (2002). Identification of a novel transporter for dicarboxylates and tricarboxylates in plant mitochondria. *J Biol Chem.*, 227, 24204-24211.
doi:10.1074/jbc.M202702200.

García-Sánchez, M.I., Gotor, C., Jacquot, JP., & Vega, J.M. (2000). Glutamate synthase from Chlamydomonas reinhardtii: Interaction studies with its substrate ferredoxin and molecular clonin. *Plant and Soil*, 221, 59-65.
doi:10.1023/A:1004715504065.

Hodges, M. (2002). Enzyme redundancy and the importance of 2-oxoglutarate in plant ammonium assimilation.
*Journal of Experimental Botany*, 53, 905-916.

Hirel, B., & Krapp, A. (2020). Nitrogen utilization in plants I biological and agronomic importance.
*Encyclopedia of Biochemistry. 3rd Edition*. Elsevier.

Mann, A.F., Fentem, P.A., & Steward, G.R. (1979). Identification of two forms of glutamine synthetase in barley (*Hordeum vulgare* L.). *Biochemical and Biophysical Research Communications*, 88, 512-521.

Wallsgrove, R.M., Lea, P.J., & Miflin, B.J. (1979). Distribution of the enzymes of nitrogen assimilation within the pea leaf cell. *Plant Physiology*, 63, 232-236.

Yamaya, T., & Kusano, M. (2014). Evidence supporting distinct functions of three cytosolic glutamine synthetases and two NADH-glutamate synthases. *Journal of Experimental Botany*, 19, 5519-5525.

Miranda-Vizuete, A., Damdimopoulos, A.E., Gustafsson, J., & Spyrou, G. (1997). Cloning, expression, and characterization of a novel Escherichia coli thioredoxin. *J Biol Chem*, 49, 30841-30847.
doi:10.1074/jbc.272.49.30841. PMID: 9388228.

Q29

Further reading

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The corrections made in this section will be reviewed and approved by a journal production editor. The newly added/removed references and its citations will be reordered and rearranged by the production team.

Chen, R.D. (1998). Plant NADP-dependent isocitrate dehydrogenases are predominantly localized in the cytosol. *Planta*, 207, 280-285.

Chen, R.D., & Gadal, P. (1990a). Do the mitochondria provide the 2-oxoglutarate needed for glutamate synthesis in higher plants? *Plant Physiology and Biochemistry*, 28, 141-145.
Chen, R.D., & Gadal, P. (1990b). Structure, functions and regulation of NAD and NADP dependent isocitrate dehydrogenases in higher plants and in other organisms. Plant Physiology and Biochemistry, 28, 411–427.

Chen, R.D., Le Marechal, P., Vidal, J., & Gadal, P. (1988). Purification and comparative properties of the cytosolic isocitrate dehydrogenase (NADP) from pea (*Pisum sativum*) roots and leaves. European Journal of Biochemistry, 175, 565–572.

Damdimopoulos, A.E., Gustafsson, J., & Spyrou, G. (1997). Cloning, expression, and characterization of a novel Escherichia coli thioredoxin. The Journal of Biological Chemistry, 272, 30841–30847.

Gotor, C., Jacquot, J.P., & Vega, J.M. (2000). Glutamate synthase from *Chlamydomonas reinhardtii*: Interaction studies with its substrate ferredoxin and molecular cloning. Plant and Soil, 221, 59–65.

Jacquot, J.-P., Gadal, P., Nishizawa, A.N., Yee, B.C., Crawford, N.A., & Buchanan, B.B. (1984). Enzyme regulation in C4 photosynthesis: Mechanism of activation of NADP-malate dehydrogenase by reduced thioredoxin. Archives of Biochemistry and Biophysics, 228, 170–178.

Mann, A.F., Fentem, P.A., & Stewart, G.R. (1980). Tissue localization of barley (*Hordeum vulgare* L.) glutamine synthetase isoenzymes. FEBS Letters, 110, 265–267.

Mittard, V., Blackledge, M.J., Stein, M., Jacquot, J.P., Marion, D., & Lancelin, J.M. (1997). NMR solution structure of an oxidised thioredoxin h form the eukaryotic alga *Chlamydomonas reinhardtii*. European Journal of Biochemistry, 243, 374–378.

Pérez-Pérez, M.-E., Mauriès, A., Maes, A., Tourasse, N.J., Hamon, M., & Lemaire, S.D., et al. (2017). The deep thioredoxome in *Chlamydomonas reinhardtii*: New insights into redox regulation. Molecular Plant, 10, 1107–1125.

**Keywords:** Fructose bisphosphatase; Glutamine synthetase; GOGAT; Isocitrate dehydrogenase; NADP-malate dehydrogenase; Nitrogen assimilation; PEP carboxylase; Photosynthesis; Redox regulation; Thioredoxin

**Queries and Answers**

Q1

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**Answer:** Please find a better quality image for Fig 4

Q2

**Query:** Please check whether the suggested running head "Scientific contributions of Pierre Gadal and his lab" is appropriate for this chapter.

**Answer:** This is correct
Q3

**Query:** Please note that "Frederic" has been treated as initial and "De Lamotte" has been treated as surname in the author name "Frederic De Lamotte". Please check and confirm if it is correct.

**Answer:** This is OK

Q4

**Query:** Please note that "Stephane D." has been treated as initial and "Lemaire" has been treated as surname in the author name "Stephane D. Lemaire". Please check and confirm if it is correct.

**Answer:** Correct

Q5

**Query:** Please check that we have captured all author names and affiliation details correctly.

**Answer:**

Q6

**Query:** Please provide a affiliation details for the author "Tatsuo Sugiyama".

**Answer:**

Tatsuo Sugiyama is now retired from Nagoya University. The only supplementary information I could provide is his private address: cedertree@nifty.com

Q7

**Query:** Please check whether the hierarchy of the section levels is appropriate as given in this chapter.

**Answer:** Correct

Q8

**Query:** Ref. "Miranda-Vizuete et al., 1997" is cited in text but not provided in the reference list. Please provide details in the list or delete the citation from the text.

**Answer:** Done

Q9

**Query:** The citation "Jacquot et al., 1997" has been changed to "Jacquot, Lopez-Jaramillo, Miginiac-Maslow, Lemaire, Cherfils, Chueca, et al., 1997" to match the author name/date in the reference list. Please check if the change is fine in this occurrence and modify the subsequent occurrences, if necessary.

**Answer:** Correct
Q10

**Query:** The citation "Mittard et al., 1994" has been changed to "Mittard et al., 1995" to match the author name/date in the reference list. Please check if the change is fine in this occurrence and modify the subsequent occurrences, if necessary.

**Answer:** Correct

Q11

**Query:** Ref. "Garcia-Sanchez et al., 2000" is cited in text but not provided in the reference list. Please provide details in the list or delete the citation from the text.

**Answer:** Citation added in the list according to : García-Sánchez, M.I., Gotor, C., Jacquot, JP. *et al*. Glutamate synthase from Chlamydomonas reinhardtii: Interaction studies with its substrate ferredoxin and molecular cloning. *Plant and Soil* **221**, 59–65 (2000). https://doi.org/10.1023/A:1004715504065

Q12

**Query:** The citation "Lemaire et al., 1999" has been changed to "Lemaire, Hours, et al., 1999; Lemaire, Keryer, et al., 1999" to match the author name/date in the reference list. Please check if the change is fine in this occurrence and modify the subsequent occurrences, if necessary.

**Answer:** Correct

Q13

**Query:** The citation "Chen et al., 1989" has been changed to "Chen, Bismuth, Champigny, & Gadal, 1989; Chen, Bismuth, Issakidis, et al., 1989" to match the author name/date in the reference list. Please check if the change is fine in this occurrence and modify the subsequent occurrences, if necessary.

**Answer:** Correct

Q14

**Query:** Please provide chapter title followed by author names in place of "Chapter 4".

**Answer:** Chapter 4: Glutamate synthase and amino acid synthesis in higher plants. Author: Akira Suzuk

Q15

**Query:** The citation "Hoagland (1938)" has been changed to "Hoagland and Arnon (1938)" to match the author name/date in the reference list. Please check if the change is fine in this occurrence and modify the subsequent occurrences, if necessary.

**Answer:** Correct

Q16

**Query:** The citation "Lowry, 1951" has been changed to "Lowry, Rosenbrowgh, Farr, & Randall, 1951" to match the author name/date in the reference list. Please check if the change is fine in this occurrence and modify the subsequent occurrences, if necessary.

**Answer:** Correct
Q17

**Query:** Please provide chapter title followed by author names in place of "Chapter 3".

**Answer:** Chapter 3: Scientific contributions of Pierre Gadal and his Lab. Nitrogen metabolism pathways and regulation - Akira Suzuki's recollections. Author: Akira Suzuki

Q18

**Query:** Ref. "Hodges, 2002" is cited in text but not provided in the reference list. Please provide details in the list or delete the citation from the text.

**Answer:** Citation added in the list and inserted in text

Q19

**Query:** Ref. "Hirel and Krapp, 2019" is cited in text but not provided in the reference list. Please provide details in the list or delete the citation from the text.

**Answer:** Date corrected (2020 instead of 209) and reference added in the list and in text

Q20

**Query:** Ref. "Mann et al. 1979" is cited in text but not provided in the reference list. Please provide details in the list or delete the citation from the text.

**Answer:** Done

Q21

**Query:** Ref. "Wallsgrove et al., 1979" is cited in text but not provided in the reference list. Please provide details in the list or delete the citation from the text.

**Answer:** Done

Q22

**Query:** Ref. "McNally et al. (1981)" is cited in text but not provided in the reference list. Please provide details in the list or delete the citation from the text.

**Answer:** Date corrected (1983 instead of 1981) and connected to the reference in the list

Q23

**Query:** Ref. "Yamaya and Kusano 2014" is cited in text but not provided in the reference list. Please provide details in the list or delete the citation from the text.

**Answer:** Done
Q24

**Query:** The citation "Cullimore et al., 1983" has been changed to "Cullimore, Gebhardt, Saarelainen, Miflin, Idler, & Barker, 1984" to match the author name/date in the reference list. Please check if the change is fine in this occurrence and modify the subsequent occurrences, if necessary.

**Answer:** Correct

Q25

**Query:** Ref. "Picault et al., 2002" is cited in text but not provided in the reference list. Please provide details in the list or delete the citation from the text.

**Answer:** I added the reference in the list according to this :

Picault N, Palmieri L, Pisano I, Hodges M, Palmieri F. Identification of a novel transporter for dicarboxylates and tricarboxylates in plant mitochondria. Bacterial expression, reconstitution, functional characterization, and tissue distribution. J Biol Chem. 2002 Jul 5;277(27):24204-11.

doi: 10.1074/jbc.M202702200.

Epub 2002 Apr 26. PMID: 11978797.

Q26

**Query:** Please check whether the inserted volume and page numbers are appropriate in the reference "Quilleré and Hirel (2020)".

**Answer:** Correct

Q27

**Query:** Please provide publisher name for the reference "Lockard (1959)".

**Answer:** Done

Q28

**Query:** Please check whether the edit made to the volume number ans the inserted page number are appropriate in the reference "Ziegler et al. (2003)".

**Answer:** Correct

Q29

**Query:** Further reading section contains references that are not cited in manuscript text. Please cite the references or confirm if we could delete it? Further reading will be retained if the references are not cited or deleted.

**Answer:**