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N Use By Plants
Nitrate Assimilation
Ammonia Assimilation
Glu, Gln, Asn, Gly, Ser
Aminotransferases
Asp, Ala, GABA
Val, Leu, Ileu, Thr, Lys
Pro, Arg, Orn
Polyamines
Non-protein AAs
Alkaloids
Sulfate Assimilation
Cys, Met, AdoMet, ACC
His, Phe, Tyr, Tryp
Secondary Products
Onium Compounds
Enzymes
Methods
Simulation
References
HORT640 - Metabolic Plant Physiology

References, tungstate or tungsten

Anderson LA, McNairn E, Leubke T, Pau RN, Boxer DH. ModE-dependent molybdate regulation of the molybdenum cofactor operon moa in Escherichia coli J. Bacteriol. 182: 7035-7043 (2000).

Bevers LE, Hagedoorn PL, Krijger GC, Hagen WR. Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters. J. Bacteriol. 188: 6498-6505 (2006).

Bevers LE, Hagedoorn PL, Santamaria-Araujo JA, Magalon A, Hagen WR, Schwarz G. Function of MoaB proteins in the biosynthesis of the molybdenum and tungsten cofactors. Biochemistry 47: 949-956 (2008).

Brondino CD, Passeggi MCG, Caldeira J, Almendra MJ, Feio MJ, Moura JJG, Moura I. Incorporation of either molybdenum or tungsten into formate dehydrogenase from Desulfovibrio alaskensis NCIMB 13491; EPR assignment of the proximal iron- sulfur cluster to the pterin cofactor in formate dehydrogenases from sulfate- reducing bacteria. J. Biol. Inorg. Chem. 9: 145-151 (2004).

De Bok FA, Hagedoorn PL, Silva PJ, Hagen WR, Schiltz E, Fritsche K, Stams AJ. Two W-containing formate dehydrogenases (CO2-reductases) involved in syntrophic propionate oxidation by Syntrophobacter fumaroxidans. Eur. J. Biochem. 270: 2476-2485 (2003).

De S, Perkins M, Dutta SK. Nitrate reductase gene involvement in hexachlorobiphenyl dechlorination by Phanerochaete chrysosporium. J. Hazard. Mater. 135: 350-354 (2006).

Dobbek H, Huber R. The molybdenum and tungsten cofactors: A crystallographic view. Met. Ions Biol. Syst. 39: 227-263 (2002).

Ferry JG. Formate dehydrogenase. FEMS Microbiol. Rev. 7: 377-382 (1990).

Gates AJ, Hughes RO, Sharp SR, Millington PD, Nilavongse A, Cole JA, Leach ER, Jepson B, Richardson DJ, Butler CS. Properties of the periplasmic nitrate reductases from Paracoccus pantotrophus and Escherichia coli after growth in tungsten-supplemented media. FEMS Microbiol. Lett. 220: 261-269 (2003).

Hille R. Molybdenum and tungsten in biology. Trends Biochem. Sci. 27: 360-367 (2002).

Jiang J, Holm RH. Reaction systems related to dissimilatory nitrate reductase: nitrate reduction mediated by bis(dithiolene)tungsten complexes. Inorg. Chem. 44: 1068-1072 (2005).

Kisker C, Schindelin H, Rees DC. Molybdenum-cofactor-containing enzymes: structure and mechanism. Annu. Rev. Biochem. 66: 233-267 (1997).

L'vov NP, Nosikov AN, Antipov AN. Tungsten-containing enzymes. Biochem. (Moscow) 67: 196-200 (2002).

Laukel M, Chistoserdova L, Lidstrom ME, Vorholt JA. The tungsten-containing formate dehydrogenase from Methylobacterium extorquens AM1: purification and properties. Eur. J. Biochem. 270: 325-333 (2003).

Morozkina EV, Nosikov AN, Zvyagilskaya RA, L'vov NP. Isolation, purification, and characterization of nitrate reductase from a salt-tolerant Rhodotorula glutinis yeast strain grown in the presence of tungsten. Biochemistry (Mosc.) 70: 809-814 (2005).

Moura JJ, Brondino CD, Trincao J, Romao MJ. Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases. J. Biol. Inorg. Chem. 9: 791-799 (2004).

Nosikov AN, Chichikalo EV, Golubeva LI, Zvyagilskaya RA, L'vov NP. Stimulation of nitrate reductase activity of the salt-tolerant yeast Rhodotorula glutinis by tungsten in the presence of molybdenum. Biochemistry (Mosc.) 65: 204-207 (2000).

Pollock VV, Conover RC, Johnson MK, Barber MJ. Bacterial expression of the molybdenum domain of assimilatory nitrate reductase: production of both the functional molybdenum-containing domain and the nonfunctional tungsten analog. Arch. Biochem. Biophys. 403: 237-248 (2002).

Raaijmakers H, Macieira S, Dias J, Teixeira S, Bursakov S, Huber R, Moura J, Moura I, Romao M. Gene sequence and the 1.8 A crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas. Structure (Camb.) 10: 1261 (2002).

Rauh D, Graentzdoerffer A, Granderath K, Andreesen JR, Pich A. Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum: isolation, characterization and molecular analysis. Eur. J. Biochem. 271: 212-219 (2004).

Reda T, Plugge CM, Abram NJ, Hirst J. Reversible interconversion of carbon dioxide and formate by an electroactive enzyme. Proc. Natl. Acad. Sci. U.S.A. 105: 10654-10658 (2008).

Singh S, Chakravarty D, Singh HN. Mutational replacement of molybdenum by vanadium in assimilation of N2 or NO3- as nitrogen source in the cyanobacterium Nostoc muscorum. Biochem. Mol. Biol. Int. 29: 1083-1093 (1993).

Sodeinde OA, Kindle KL. Homologous recombination in the nuclear genome of Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. U.S.A. 90: 9199-9203 (1993).

Svab Z, Hajdukiewicz P, Maliga P. Stable transformation of plastids in higher plants. Proc. Natl. Acad. Sci. U.S.A. 87: 8526-8530 (1990).

Thiel T, Pratte B, Zahalak M. Transport of molybdate in the cyanobacterium Anabaena variabilis ATCC 29413. Arch. Microbiol. 179: 50-56 (2002).

Vergnes A, Gouffi-Belhabich K, Blasco F, Giordano G, Magalon A. Involvement of the molybdenum cofactor biosynthetic machinery in the maturation of the Escherichia coli nitrate reductase A. J. Biol. Chem. 279: 41398-41403 (2004).

Watts CA, Ridley H, Condie KL, Leaver JT, Richardson DJ, Butler CS. Selenate reduction by Enterobacter cloacae SLD1a-1 is catalysed by a molybdenum-dependent membrane-bound enzyme that is distinct from the membrane- bound nitrate reductase. FEMS Microbiol. Lett. 228: 273-279 (2003).

Wu Q, Knowles R. Cellular regulation of nitrate uptake in denitrifying Flexibacter canadensis. Can. J. Microbiol. 40: 576-582 (1994).

Wu S, Lu Q, Kriz AL, Harper JE. Identification of cDNA clones corresponding to two inducible nitrate reductase genes in soybean: analysis in wild-type and nr1 mutant. Plant Mol. Biol. 29: 491-506 (1995).

Zheng ZL, Yang Z, Jang JC, Metzger JD. Phytochromes A1 and B1 have distinct functions in the photoperiodic control of flowering in the obligate long-day plant Nicotiana sylvestris. Plant Cell Environ. 29: 1673-1685 (2006).

Number of references = 30

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David Rhodes
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