|
HORT640 - Metabolic Plant Physiology
References, molybdate or molybdenum or molybdo
Aguilar M, Kalakoutskii K, Cardenas J, Fernandez E. Direct transfer of molybdopterin cofactor to aponitrate reductase from a carrier protein in Chlamydomonas reinhardtii. FEBS Lett. 307: 162-163 (1992).
Aguilar MR, Cardenas J, Fernandez E. Regulation of molybdenum cofactor species in the green alga Chlamydomonas reinhardtii. Biochim. Biophys. Acta 1073: 463-469 (1991).
Akaba S, Leydecker MT, Moureaux T, Oritani T, Koshiba T. Aldehyde oxidase in wild type and aba1 mutant leaves of Nicotiana plumbaginifolia. Plant Cell Physiol. 39: 1281-1286 (1998).
Amrani L, Primus J, Glatigny A, Arcangeli L, Scazzocchio C, Finnerty V. Comparison of the sequences of the Aspergillus nidulans hxB and Drosophila melanogaster ma-l genes with nifS from Azotobacter vinelandii suggests a mechanism for the insertion of the terminal sulphur atom in the molybdopterin cofactor. Mol. Microbiol. 38: 114-125 (2000).
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).
Anderson LJ, Richardson DJ, Butt JN. Using direct electrochemistry to probe rate limiting events during nitrate reductase turnover. Faraday Discuss. 116: 155-169 (2000).
Anke M, Seifert M. The biological and toxicological importance of molybdenum in the environment and in the nutrition of plants, animals and man. Part 1: Molybdenum in plants. Acta Biol. Hung. 58: 311-324 (2007).
Antipov AN, Lyalikova NN, Khijniak TV, L'vov NP. Molybdenum-free nitrate reductases from vanadate-reducing bacteria. FEBS Lett. 441: 257-260 (1998).
Antipov AN, Lyalikova NN, Khijniak TV, L'vov NP. Vanadate reduction by molybdenum-free dissimilatory nitrate reductases from vanadate-reducing bacteria. IUBMB Life 50: 39-42 (2000).
Antipov AN, Lyalikova NN, Khiznjak TV, L'vov NP. Some properties of dissimilatory nitrate reductases lacking molybdenum and molybdenum cofactor. Biochemistry (Mosc.) 64: 483-487 (1999).
Antipov AN, Morozkina EV, Sorokin DY, Golubeva LI, Zvyagilskaya RA, L'vov NP. Characterization of molybdenum-free nitrate reductase from haloalkalophilic bacterium Halomonas sp. strain AGJ 1-3. Biochemistry (Mosc.) 70: 799-803 (2005).
Antipov AN, Sorokin DY, L'vov NP, Kuenen JG. New enzyme belonging to the family of molybdenum-free nitrate reductases. Biochem. J. 369: 185-189 (2003).
Armienta-Aldana E, Gonzalez De La Vara LE. Acid phosphatases from beet root (Beta vulgaris) plasma membranes. Physiol. Plant. 121: 223-230 (2004).
Arnoux P, Sabaty M, Alric J, Frangioni B, Guigliarelli B, Adriano JM, Pignol D. Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase. Nat. Struct. Biol. 10: 928-934 (2003).
Augier V, Asso M, Guigliarelli B, More C, Bertrand P, Santini CL, Blasco F, Chippaux M, Giordano G. Removal of the high-potential [4Fe-4S] center of the beta-subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutated enzymes. Biochemistry 32: 5099-5108 (1993).
Bachmann M, Shiraishi N, Campbell WH, Yoo BC, Harmon AC, Huber SC. Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase. Plant Cell 8: 505-517 (1996).
Bageshwar UK, Raina R, Das HK. Characterization of a spontaneous mutant of Azotobacter vinelandii in which vanadium-dependent nitrogen fixation is not inhibited by molybdenum. FEMS Microbiol. Lett. 162: 161-167 (1998).
Baker KP, Boxer DH. Regulation of the chlA locus of Escherichia coli K12: involvement of molybdenum cofactor. Mol. Microbiol. 5: 901-907 (1991).
Baltes N, Hennig-Pauka I, Jacobsen I, Gruber AD, Gerlach GF. Identification of dimethyl sulfoxide reductase in Actinobacillus pleuropneumoniae and its role in infection. Infect. Immun. 71: 6784-6792 (2003).
Barabas NK, Omarov RT, Erdei L, Lips SH. Distribution of the Mo-enzymes aldehyde oxidase, xanthine dehydrogenase and nitrate reductase in maize (Zea mays L.) nodal roots as affected by nitrogen and salinity. Plant Sci. 155: 49-58 (2000).
Barber MJ, Neame PJ. A conserved cysteine in molybdenum oxotransferases. J. Biol. Chem. 265: 20912-20915 (1990).
Barbier GG, Campbell WH. Viscosity effects on eukaryotic nitrate reductase activity. J. Biol. Chem. 280: 26049-26054 (2005).
Barbier GG, Joshi RC, Campbell ER, Campbell WH. Purification and biochemical characterization of simplified eukaryotic nitrate reductase expressed in Pichia pastoris. Protein Expr. Purif. 37: 61-71 (2004).
Basu P, Nemykin VN, Sengar RS. Syntheses, spectroscopy, and redox chemistry of encapsulated Oxo-Mo(V) centers: implications for pyranopterin-containing molybdoenzymes. Inorg. Chem. 42: 7489-7501 (2003).
Bender KS, Shang C, Chakraborty R, Belchik SM, Coates JD, Achenbach LA. Identification, characterization, and classification of genes encoding perchlorate reductase. J. Bacteriol. 187: 5090-5096 (2005).
Bennett B, Charnock JM, Sears HJ, Berks BC, Thomson AJ, Ferguson SJ, Garner CD, Richardson DJ. Structural investigation of the molybdenum site of the periplasmic nitrate reductase from Thiosphaera pantotropha by X-ray absorption spectroscopy. Biochem. J. 317: 557-563 (1996).
Berks BC, Richardson DJ, Robinson C, Reilly A, Aplin RT, Ferguson SJ. Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha. Eur. J. Biochem. 220: 117-124 (1994).
Bertero MG, Rothery RA, Palak M, Hou C, Lim D, Blasco F, Weiner JH, Strynadka NCJ. Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nat. Struct. Biol. 10: 681-687 (2003).
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).
Blasco F, Dos Santos JP, Magalon A, Frixon C, Guigliarelli B, Santini CL, Giordano G. NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli. Mol. Microbiol. 28: 435-447 (1998).
Blasco F, Iobbi C, Giordano G, Chippaux M, Bonnefoy V. Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer. Mol. Gen. Genet. 218: 249-256 (1989).
Blasco F, Iobbi C, Ratouchniak J, Bonnefoy V, Chippaux M. Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon. Mol. Gen. Genet. 222: 104-111 (1990).
Blasco F, Pommier J, Augier V, Chippaux M, Giordano G. Involvement of the narJ or narW gene product in the formation of active nitrate reductase in Escherichia coli. Mol. Microbiol. 6: 221-230 (1992).
Bonnard N, Tresierra-Ayala A, Bedmar EJ, Delgado MJ. Molybdate-dependent expression of the periplasmic nitrate reductase in Bradyrhizobium japonicum. Biochem. Soc. Trans. 33: 127-129 (2005).
Boxer DH. Involvement of the chlorate resistance loci and the molybdenum cofactor in the biosynthesis of the Escherichia coli nitrate reductase. In "Molecular and Genetic Aspects of Nitrate Assimilation" (JL Wray, JR Kinghorn eds) Oxford Science Publications, Oxford, pp. 27-39 (1989).
Bozzo GG, Raghothama KG, Plaxton WC. Purification and characterization of two secreted purple acid phosphatase isozymes from phosphate-starved tomato (Lycopersicon esculentum) cell cultures. Eur. J. Biochem. 269: 6278-6286 (2002).
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).
Brooijmans RJ, de Vos WM, Hugenholtz J. Lactobacillus plantarum WCFS1 electron transport chains. Appl. Environ. Microbiol. 75: 3580-3585 (2009).
Brychkova G, Alikulov Z, Fluhr R, Sagi M. A critical role for ureides in dark and senescence-induced purine remobilization is unmasked in the Atxdh1 Arabidopsis mutant. Plant J. 54: 496-509 (2008).
Buc J, Santini CL, Blasco F, Giordani R, Cardenas ML, Chippaux M, Cornish-Bowden A, Giordano G. Kinetic studies of a soluble alpha beta complex of nitrate reductase A from Escherichia coli. Use of various alpha beta mutants with altered beta subunits. Eur. J. Biochem. 234: 766-772 (1995).
Buchanan G, Kuper J, Mendel RR, Schwarz G, Palmer T. Characterisation of the mob locus of Rhodobacter sphaeroides WS8: mobA is the only gene required for molybdopterin guanine dinucleotide synthesis. Arch. Microbiol. 176: 62-68 (2001).
Burgdorf T, Bommer D, Bowien B. Involvement of an unusual mol operon in molybdopterin cofactor biosynthesis in Ralstonia eutropha. J. Mol. Microbiol. Biotechnol. 3: 619-629 (2001).
Bursakov SA, Carneiro C, Almendra MJ, Duarte RO, Caldeira J, Moura I, Moura JJ. Enzymatic properties and effect of ionic strength on periplasmic nitrate reductase (NAP) from Desulfovibrio desulfuricans ATCC 27774. Biochem. Biophys. Res. Commun. 239: 816-822 (1997).
Butler CS, Charnock JM, Bennett B, Sears HJ, Reilly AJ, Ferguson SJ, Garner CD, Lowe DJ, Thomson AJ, Berks BC, Richardson DJ. Models for molybdenum coordination during the catalytic cycle of periplasmic nitrate reductase from Paracoccus denitrificans derived from EPR and EXAFS spectroscopy. Biochemistry 38: 9000-9012 (1999).
Butler CS, Charnock JM, Garner CD, Thomson AJ, Ferguson SJ, Berks BC, Richardson DJ. Thiocyanate binding to the molybdenum centre of the periplasmic nitrate reductase from Paracoccus pantotrophus. Biochem. J. 352: 859-864 (2000).
Butler CS, Fairhurst SA, Ferguson SJ, Thomson AJ, Berks BC, Richardson DJ, Lowe DJ. Mo(V) co-ordination in the periplasmic nitrate reductase from Paracoccus pantotrophus probed by electron nuclear double resonance (ENDOR) spectroscopy. Biochem. J. 363: 817-823 (2002).
Butler CS, Ferguson SJ, Berks BC, Thomson AJ, Cheesman MR, Richardson DJ. Assignment of haem ligands and detection of electronic absorption bands of molybdenum in the di-haem periplasmic nitrate reductase of Paracoccus pantotrophus. FEBS Lett. 500: 71-74 (2001).
Campbell WH. Nitrate reductase structure, function and regulation: bridging the gap between biochemistry and physiology. Annu. Rev. Plant Physiol. Plant Mol. Biol. 50: 277-303 (1999).
Campbell WH. Structure and function of eukaryotic NAD(P)H:nitrate reductase. Cell Mol. Life Sci. 58: 194-204 (2001).
Carrano CJ, Chohan BS, Hammes BS, Kail BW, Nemykin VN, Basu P. Donor atom dependent geometric isomers in mononuclear oxo-molybdenum(V) complexes: Implications for coordinated endogenous ligation in molybdoenzymes. Inorg. Chem. 42: 5999-6007 (2003).
Cerqueira NM, Gonzalez PJ, Brondino CD, Romao MJ, Romao CC, Moura I, Moura JJ. The effect of the sixth sulfur ligand in the catalytic mechanism of periplasmic nitrate reductase. J. Comput. Chem. 30: 2466-2484 (2009).
Chan CS, Howell JM, Workentine ML, Turner RJ. Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli. Biochem. Biophys. Res. Commun. 343: 244-151 (2006).
Chang PK, Ehrlich KC, Linz JE, Bhatnagar D, Cleveland TE, Bennett JW. Characterization of the Aspergillus parasiticus niaD and niiA gene cluster. Curr. Genet. 30: 68-75 (1996).
Chen GX, Fu XP, Lips SH, Sagi M. Control of plant growth resides in the shoot, and not in the root, in reciprocal grafts of flacca and wild-type tomato (Lysopersicon esculentum), in the presence and absence of salinity stress. Plant Soil 256: 205-215 (2003).
Chiang RC, Cavicchioli R, Gunsalus RP. Identification and characterization of narQ, a second nitrate sensor for nitrate-dependent gene regulation in Escherichia coli. Mol. Microbiol. 6: 1913-1923 (1992).
Clark MB, Mills HA, Robacker CD, Latimer JG. Influence of nitrate: ammonium ratios on growth and elemental concentration in two azalea cultivars. J. Plant Nutr. 26: 2503-2520 (2003).
Coddington A. Biochemical studies on the nit mutants of Neurospora crassa. Mol. Gen. Genet. 145: 195-206 (1976).
Cooney JJ, Carducci MD, McElhaney AE, Selby HD, Enemark JH. New oxovanadium bis(1,2-dithiolate) compounds that mimic the hydrogen-bonding interactions at the active sites of mononuclear molybdenum enzymes. Inorg. Chem. 41: 7086-7093 (2002).
Correia C, Besson S, Brondino CD, Gonzalez PJ, Fauque G, Lampreia J, Moura I, Moura JJ. Biochemical and spectroscopic characterization of the membrane-bound nitrate reductase from Marinobacter hydrocarbonoclasticus 617. J. Biol. Inorg. Chem. 13: 1321-1333 (2008).
Creevey NL, McEwan AG, Hanson GR, Bernhardt PV. Thermodynamic characterization of the redox centers within dimethylsulfide dehydrogenase. Biochemistry 47: 3770-3776 (2008).
Curatti L, Hernandez JA, Igarashi RY, Soboh B, Zhao D, Rubio LM. In vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified proteins. Proc. Natl. Acad. Sci. U.S.A. 104: 17626-17631 (2007).
Dahl C. Insertional gene inactivation in a phototrophic sulphur bacterium: APS-reductase-deficient mutants of Chromatium vinosum. Microbiology 142: 3363-3372 (1996).
Daniel-Vedele F, Dorbe MF, Caboche M, Rouze P. Cloning and analysis of the tomato nitrate reductase-encoding gene: protein domain structure and amino acid homologies in higher plants. Gene 85: 371-380 (1989).
Danielsson H, Stenklo TK, Karlsson J, Nilsson T. A gene cluster for chlorate metabolism in Ideonella dechloratans. Appl. Environ. Microbiol. 69: 5585-5592 (2003).
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 Jong GAH, Tang JA, Bos P, de Vries S, Kuenen JG. Purification and characterization of a sulfite:cytochrome c oxidoreductase from Thiobacillus acidophilus. J. Mol. Catal. B. Enzym. 8: 61-67 (2000).
De la Rosa MA. Assimilatory nitrate reductase from the green alga Ankistrodesmus braunii. Mol. Cell Biochem. 50: 65-74 (1983).
De S, Perkins M, Dutta SK. Nitrate reductase gene involvement in hexachlorobiphenyl dechlorination by Phanerochaete chrysosporium. J. Hazard. Mater. 135: 350-354 (2006).
Dean JV, Harper JE. The conversion of nitrite to nitrogen oxide(s) by the constitutive NAD(P)H-nitrate reductase enzyme from soybean. Plant Physiol. 88: 389-395 (1988).
Delgado MJ, Tresierra-Ayala A, Talbi C, Bedmar EJ. Functional characterization of the Bradyrhizobium japonicum modA and modB genes involved in molybdenum transport. Microbiology 152: 199-207 (2006).
Dias JM, Bursakov S, Carneiro C, Moura JJ, Moura I, Romao MJ. Crystallization and preliminary X-ray analysis of a nitrate reductase from Desulfovibrio desulfuricans ATCC 27774. Acta Crystallogr. D. Biol. Crystallogr. 55: 877-879 (1999).
Dias JM, Than ME, Humm A, Huber R, Bourenkov GP, Bartunik HD, Bursakov S, Calvete J, Caldeira J, Carneiro C, Moura JJ, Moura I, Romao MJ. Crystal structure of the first dissimilatory nitrate reductase at 1.9 A solved by MAD methods. Structure 7: 65-79 (1999).
Dobbek H, Huber R. The molybdenum and tungsten cofactors: A crystallographic view. Met. Ions Biol. Syst. 39: 227-263 (2002).
Douglas P, Morrice N, MacKintosh C. Identification of a regulatory phosphorylation site in the hinge 1 region of nitrate reductase from spinach (Spinacea oleracea) leaves. FEBS Lett. 377: 113-117 (1995).
Dridge EJ, Richardson DJ, Lewis RJ, Butler CS. Developing structure-based models to predict substrate specificity of D-group (type II) molybdenum enzymes: application to a molybdo-enzyme of unknown function from Archaeoglobus fulgidus. Biochem. Soc. Trans. 34: 118-121 (2006).
Du S, Zhang Y, Lin X, Wang Y, Tang C. Regulation of nitrate reductase by nitric oxide in Chinese cabbage pakchoi (Brassica chinensis L.). Plant Cell Environ. 31: 195-204 (2008).
Eaves DJ, Palmer T, Boxer DH. The product of the molybdenum cofactor gene mobB of Escherichia coli is a GTP-binding protein. Eur. J. Biochem. 246: 690-697 (1997).
Eckardt NA. Moco mojo: crystal structure reveals essential features of eukaryotic assimilatory nitrate reduction. Plant Cell 17: 1029-1031 (2005).
Eilers T, Schwarz G, Brinkmann H, Witt C, Richter T, Nieder J, Koch B, Hille R, Hansch R, Mendel RR. Identification and biochemical characterization of Arabidopsis thaliana sulfite oxidase - A new player in plant sulfur metabolism. J. Biol. Chem. 276: 46989-46994 (2001).
Elliott SJ, Hoke KR, Heffron K, Palak M, Rothery RA, Weiner JH, Armstrong FA. Voltammetric studies of the catalytic mechanism of the respiratory nitrate reductase from Escherichia coli: How nitrate reduction and inhibition depend on the oxidation state of the active site. Biochemistry 43: 799-807 (2004).
Enemark JH, Cosper MM. Molybdenum enzymes and sulfur metabolism. Met. Ions Biol. Syst. 39: 621-654 (2002).
Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF. Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Proc. Natl. Acad. Sci. U.S.A. 97: 10723-10728 (2000).
Falciani F, Terao M, Goldwurm S, Ronchi A, Gatti A, Minoia C, Li Calzi M, Salmona M, Cazzaniga G, Garattini E. Molybdenum(VI) salts convert the xanthine oxidoreductase apoprotein into the active enzyme in mouse L929 fibroblastic cells. Biochem. J. 298: 69-77 (1994).
Falk KL, Guerra DJ. Coenzyme A biosynthesis in plants: partial purification and characterization of pantothenate kinase from spinach. Arch. Biochem. Biophys. 301: 424-430 (1993).
Fedtke I, Kamps A, Krismer B, Gotz F. The nitrate reductase and nitrite reductase operons and the narT gene of Staphylococcus carnosus are positively controlled by the novel two-component system NreBC. J. Bacteriol. 184: 6624-6634 (2002).
Feelisch M, Fernandez BO, Bryan NS, Garcia-Saura MF, Bauer S, Whitlock DR, Ford PC, Janero DR, Rodriguez J, Ashrafian H. Tissue processing of nitrite in hypoxia: an intricate interplay of nitric oxide-generating and -scavenging systems. J. Biol. Chem. 283: 33927-33934 (2008).
Ferguson SJ. Nitrogen cycle enzymology. Curr. Opin. Chemical Biol. 2: 182-193 (1998).
Fernandez E, Cardenas J. In vitro complementation of assimilatory NAD(P)H-nitrate reductase from mutants of Chlamydomonas reinhardii. Biochim. Biophys. Acta 657: 1-12 (1981).
Ferry JG. Formate dehydrogenase. FEMS Microbiol. Rev. 7: 377-382 (1990).
Fetzner S. Enzymes involved in the aerobic bacterial degradation of N-heteroaromatic compounds: molybdenum hydroxylases and ring-opening 2,4-dioxygenases. Naturwissenschaften 87: 59-69 (2000).
Fido RJ. Isolation and partial amino acid sequence of domains of nitrate reductase from spinach. Phytochemistry 30: 3519-3523 (1991).
Fischer K, Barbier GG, Hecht HJ, Mendel RR, Campbell WH, Schwarz G. Structural basis of eukaryotic nitrate reduction: crystal structures of the nitrate reductase active site. Plant Cell 17: 1167-1179 (2005).
Flores E, Frias JE, Rubio LM, Herrero A. Photosynthetic nitrate assimilation in cyanobacteria. Photosynth. Res. 83: 117-133 (2005).
Fourmond V, Burlat B, Dementin S, Arnoux P, Sabaty M, Boiry S, Guigliarelli B, Bertrand P, Pignol D, Leger C. Major Mo(V) EPR signature of Rhodobacter sphaeroides periplasmic nitrate reductase arising from a dead-end species that activates upon reduction. Relation to other molybdoenzymes from the DMSO reductase family. J. Phys. Chem. B. 112: 15478-15486 (2008).
Frey B, Janel G, Michelsen U, Kersten H. Mutations in the Escherichia coli fnr and tgt genes: control of molybdate reductase activity and the cytochrome d complex by fnr. J. Bacteriol. 171: 1524-1530 (1989).
Frey PA, Hegeman AD, Ruzicka FJ. The radical SAM superfamily. Crit. Rev. Biochem. Mol. Biol. 43: 63-88 (2008).
Fujinaga K, Taniguchi Y, Sun Y, Katayama S, Minami J, Matsushita O, Okabe A. Analysis of genes involved in nitrate reduction in Clostridium perfringens. Microbiology 145: 3377-3387 (1999).
Ganas P, Sachelaru P, Mihasan M, Igloi GL, Brandsch R. Two closely related pathways of nicotine catabolism in Arthrobacter nicotinovorans and Nocardioides sp. strain JS614. Arch. Microbiol. 189: 511-517 (2008).
Gangeswaran R, Lowe DJ, Eady RR. Purification and characterization of the assimilatory nitrate reductase of Azotobacter vinelandii. Biochem. J. 289: 335-342 (1993).
Garde J, Kinghorn JR, Tomsett AB. Site-directed mutagenesis of nitrate reductase from Aspergillus nidulans. Identification of some essential and some nonessential amino acids among conserved residues. J. Biol. Chem. 270: 6644-6650 (1995).
Gardlik S, Rajagopalan KV. The mechanisms of inactivation of sulfite oxidase by periodate and arsenite. J. Biol. Chem. 266: 16627-16632 (1991).
Garzon A, Li J, Flores A, Casadesus J, Stewart V. Molybdenum cofactor (chlorate-resistant) mutants of Klebsiella pneumoniae M5al can use hypoxanthine as the sole nitrogen source. J. Bacteriol. 174: 6298-6302 (1992).
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).
Gawronski JD, Benson DR. Microtiter assay for glutamine synthetase biosynthetic activity using inorganic phosphate detection. Anal. Biochem. 327: 114-118 (2004).
Gerber S, Comellas-Bigler M, Goetz BA, Locher KP. Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter. Science 321: 246-250 (2008).
Giordano G, Boxer DH, Pommier J. Molybdenum cofactor requirement for in vitro activation of apo-molybdoenzymes of Escherichia coli. Mol. Microbiol. 4: 645-650 (1990).
Giordano G, Violet M, Medani CL, Pommier J. A common pathway for the activation of several molybdoenzymes in Escherichia coli K12. Biochim. Biophys. Acta 798: 216-225 (1984).
Glaser P, Danchin A, Kunst F, Zuber P, Nakano MM. Identification and isolation of a gene required for nitrate assimilation and anaerobic growth of Bacillus subtilis. J. Bacteriol. 177: 1112-1115 (1995).
Gonzalez C, Brito N, Marzluf GA. Functional analysis by site-directed mutagenesis of individual amino acid residues in the flavin domain of Neurospora crassa nitrate reductase. Mol. Gen. Genet. 249: 456-464 (1995).
Gonzalez PJ, Rivas MG, Brondino CD, Bursakov SA, Moura I, Moura JJ. EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774. J. Biol. Inorg. Chem. 11: 609-616 (2006).
Gruber H, Goetinck SD, Kirk DL, Schmitt R. The nitrate reductase-encoding gene of Volvox carteri: map location, sequence and induction kinetics. Gene 120: 75-83 (1992).
Guo YL, Roux SJ. Partial purification and characterization of an enzyme from pea nuclei with protein tyrosine phosphatase activity. Plant Physiol. 107: 167-175 (1995).
Gutierrez JC, Santero E, Tortolero M. Ammonium repression of the nitrite-nitrate (nasAB) assimilatory operon of Azotobacter vinelandii is enhanced in mutants expressing the nifO gene at high levels. Mol. Gen. Genet. 255: 172-179 (1997).
Haenzelmann P, Hernandez HL, Menzel C, Garcia-Serres R, Huynh BH, Johnson MK, Mendel RR, Schindelin H. Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. J. Biol. Chem. 279: 34721-34732 (2004).
Hale KL, McGrath SP, Lombi E, Stack SM, Terry N, Pickering IJ, George GN, Pilon-Smits EA. Molybdenum sequestration in Brassica species. A role for anthocyanins? Plant Physiol. 126: 1391-1402 (2001).
Hansch R, Lang C, Riebeseel E, Lindigkeit R, Gessler A, Rennenberg H, Mendel RR. Plant sulfite oxidase as novel producer of H2O2: combination of enzyme catalysis with a subsequent non-enzymatic reaction step. J. Biol. Chem. 281: 6884-6888 (2006).
Hasona A, Ray RM, Shanmugam KT. Physiological and genetic analyses leading to identification of a biochemical role for the moeA (molybdate metabolism) gene product in Escherichia coli. J. Bacteriol. 180: 1466-1472 (1998).
Hasona A, Self WT, Shanmugam KT. Transcriptional regulation of the moe (molybdate metabolism) operon of Escherichia coli. Arch. Microbiol. 175: 178-188 (2001).
Hawker KL, Montague P, Kinghorn JR. Nitrate reductase and nitrite reductase transcript levels in various mutants of Aspergillus nidulans: confirmation of autogenous regulation. Mol. Gen. Genet. 231: 485-488 (1992).
Heck IS, Ninnemann H. Molybdenum cofactor biosynthesis in Neurospora crassa: biochemical characterization of pleiotropic molybdoenzyme mutants nit-7, nit-8, nit-9A, B and C. Photochem. Photobiol. 61: 54-60 (1995).
Heck IS, Schrag JD, Sloan J, Millar LJ, Kanan G, Kinghorn JR, Unkles SE. Mutational analysis of the gephyrin-related molybdenum cofactor biosynthetic gene cnxe from the lower eukaryote Aspergillus nidulans. Genetics 161: 623-632 (2002).
Hemschemeier S, Grund M, Keuntje B, Eichenlaub R. Isolation of Escherichia coli mutants defective in uptake of molybdate. J. Bacteriol. 173: 6499-6506 (1991).
Hille R. Molybdenum and tungsten in biology. Trends Biochem. Sci. 27: 360-367 (2002).
Hille R. Molybdenum enzymes containing the pyranopterin cofactor: An overview. Met. Ions Biol. Syst. 39: 187-226 (2002).
Hipkin CR, Kau DA, Cannons AC. Further characterization of the assimilatory nitrate reductase from the yeast Candida nitratophila. J. Gen. Microbiol. 139: 473-478 (1993).
Hoff T, Schnorr KM, Meyer C, Caboche M. Isolation of two Arabidopsis cDNAs involved in early steps of molybdenum cofactor biosynthesis by functional complementation of Escherichia coli mutants. J. Biol. Chem. 270: 6100-6107 (1995).
Howard JB, Rees DC. How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation. Proc. Natl. Acad. Sci. U.S.A. 103: 17088-17093 (2006).
Hu Y, Corbett MC, Fay AW, Webber JA, Hodgson KO, Hedman B, Ribbe MW. Nitrogenase Fe protein: a molybdate/homocitrate insertase. Proc. Natl. Acad. Sci. U.S.A. 103: 17125-17130 (2006).
Huber JL, Huber SC, Campbell WH, Redinbaugh MG. Reversible light/dark modulation of spinach leaf nitrate reductase activity involves protein phosphorylation. Arch. Biochem. Biophys. 296: 58-65 (1992).
Hyde GE, Crawford NM, Campbell WH. The sequence of squash NADH:nitrate reductase and its relationship to the sequences of other flavoprotein oxidoreductases. A family of flavoprotein pyridine nucleotide cytochrome reductases. J. Biol. Chem. 266: 23542-23547 (1991).
Ilbert M, Mejean V, Giudici-Orticoni MT, Samama JP, Iobbi-Nivol C. Involvement of a mate chaperone (TorD) in the maturation pathway of molybdoenzyme TorA. J. Biol. Chem. 278: 28787-28792 (2003).
Iobbi-Nivol C, Santini CL, Blasco F, Giordano G. Purification and further characterization of the second nitrate reductase of Escherichia coli K12. Eur. J. Biochem. 188: 679-687 (1990).
Jepson BJ, Mohan S, Clarke TA, Gates AJ, Cole JA, Butler CS, Butt JN, Hemmings AM, Richardson DJ. Spectropotentiometric and structural analysis of the periplasmic nitrate reductase from Escherichia coli. J. Biol. Chem. 282: 6425-6437 (2007).
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).
Johnson JL, Wuebbens MM, Mandell R, Shih VE. Molybdenum cofactor biosynthesis in humans. Identification of two complementation groups of cofactor-deficient patients and preliminary characterization of a diffusible molybdopterin precursor. J. Clin. Invest. 83: 897-903 (1989).
Jormakka M, Byrne B, Iwata S. Formate dehydrogenase - a versatile enzyme in changing environments. Curr. Opin. Struct. Biol. 13: 418-423 (2003).
Kadaba NS, Kaiser JT, Johnson E, Lee A, Rees DC. The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation. Science 321: 250-253 (2008).
Kaiser BN, Gridley KL, Ngaire Brady J, Phillips T, Tyerman SD. The role of molybdenum in agricultural plant production. Ann. Bot. (Lond.) 96: 745-754 (2005).
Kalman LV, Gunsalus RP. Nitrate- and molybdenum-independent signal transduction mutations in narX that alter regulation of anaerobic respiratory genes in Escherichia coli. J. Bacteriol. 172: 7049-7056 (1990).
Kappler U, Bennett B, Rethmeier J, Schwarz G, Deutzmann R, McEwan AG, Dahl C. Sulfite:cytochrome c oxidoreductase from Thiobacillus novellus: purification, characterization, and molecular biology of a heterodimeric member of the sulfite oxidase family. J. Biol. Chem. 275: 13202-13212 (2000).
Kappler U, Dahl C. Enzymology and molecular biology of prokaryotic sulfite oxidation. FEMS Microbiol. Lett. 203: 1-9 (2001).
Karakas E, Wilson HL, Graf TN, Xiang S, Jaramillo-Busquets S, Rajagopalan KV, Kisker C. Structural insights into sulfite oxidase deficiency. J. Biol. Chem. 280: 33506-33515 (2005).
Kisker C, Schindelin H, Rees DC. Molybdenum-cofactor-containing enzymes: structure and mechanism. Annu. Rev. Biochem. 66: 233-267 (1997).
Klaassen CD, Boles JW. Sulfation and sulfotransferases 5: the importance of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) in the regulation of sulfation. FASEB J. 11: 404-418 (1997).
Koiwai H, Akaba S, Seo M, Komano T, Koshiba T. Functional expression of two Arabidopsis aldehyde oxidases in the yeast Pichia pastoris. J. Biochem. 127: 659-664 (2000).
Kolesnikow T, Schroder I, Gunsalus RP. Regulation of narK gene expression in Escherichia coli in response to anaerobiosis, nitrate, iron, and molybdenum. J. Bacteriol. 174: 7104-7111 (1992).
Krafft T, Bowen A, Theis F, Macy JM. Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis. DNA Seq. 10: 365-377 (2000).
Kroneck PM, Abt DJ. Molybdenum in nitrate reductase and nitrite oxidoreductase. Met. Ions Biol. Syst. 39: 369-403 (2002).
Kuhlemeier CJ, Logtenberg T, Stoorvogel W, van Heugten HA, Borrias WE, van Arkel GA. Cloning of nitrate reductase genes from the cyanobacterium Anacystis nidulans. J. Bacteriol. 159: 36-41 (1984).
Kunzler K, Eichenberger W. Betaine lipids and zwitterionic phospholipids in plants and fungi. Phytochemistry 46: 883-892 (1997).
Kuper J, Palmer T, Mendel RR, Schwarz G. Mutations in the molybdenum cofactor biosynthetic protein Cnx1G from Arabidopsis thaliana define functions for molybdopterin binding, molybdenum insertion, and molybdenum cofactor stabilization. Proc. Natl. Acad. Sci. U.S.A. 97: 6475-6480 (2000).
L'vov NP, Nosikov AN, Antipov AN. Tungsten-containing enzymes. Biochem. (Moscow) 67: 196-200 (2002).
LaBrie ST, Wilkinson JQ, Tsay YF, Feldmann KA, Crawford NM. Identification of two tungstate-sensitive molybdenum cofactor mutants, chl2 and chl7, of Arabidopsis thaliana. Mol. Gen. Genet. 233: 169-176 (1992).
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).
Lebrun E, Brugna M, Baymann F, Muller D, Lievremont D, Lett MC, Nitschke W. Arsenite oxidase, an ancient bioenergetic enzyme. Mol. Biol. Evol. 20: 686-693 (2003).
Lee JH, Wendt JC, Shanmugam KT. Identification of a new gene, molR, essential for utilization of molybdate by Escherichia coli. J. Bacteriol. 172: 2079-2087 (1990).
Leimkuhler S, Klipp W. The molybdenum cofactor biosynthesis protein MobA from Rhodobacter capsulatus is required for the activity of molybdenum enzymes containing MGD, but not for xanthine dehydrogenase harboring the MPT cofactor. FEMS Microbiol. Lett. 174: 239-246 (1999).
Leydecker MT, Moureaux T, Kraepiel Y, Schnorr K, Caboche M. Molybdenum cofactor mutants, specifically impaired in xanthine dehydrogenase activity and abscisic acid biosynthesis, simultaneously overexpress nitrate reductase. Plant Physiol. 107: 1427-1431 (1995).
Lillo C, Meyer C, Ruoff P. The nitrate reductase circadian system. The central clock dogma contra multiple oscillatory feedback loops. Plant Physiol. 125: 1554-1557 (2001).
Lim BS, Willer MW, Miao M, Holm RH. Monodithiolene molybdenum(V,VI) complexes: a structural analogue of the oxidized active site of the sulfite oxidase enzyme family. J. Am. Chem. Soc. 123: 8343-8349 (2001).
Lin JT, Goldman BS, Stewart V. Structures of genes nasA and nasB, encoding assimilatory nitrate and nitrite reductases in Klebsiella pneumoniae M5al. J. Bacteriol. 175: 2370-2378 (1993).
Lin JT, Stewart V. Nitrate assimilation by bacteria. Adv. Microbiol. Physiol. 39: 1-30 (1998).
Little R, Colombo V, Leech A, Dixon R. Direct interaction of the NifL regulatory protein with the GlnK signal transducer enables the Azotobacter vinelandii NifL-NifA regulatory system to respond to conditions replete for nitrogen. J. Biol. Chem. 277: 15472-15481 (2002).
Liu MT, Wuebbens MM, Rajagopalan KV, Schindelin H. Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli. J. Biol. Chem. 275: 1814-1822 (2000).
Llamas A, Kalakoutskii KL. Molybdenum cofactor amounts in Chlamydomonas reinhardtii depend on the Nit5 gene function related to molybdate transport. Plant Cell Environ. 23: 1247-1255 (2000).
Llamas A, Tejada-Jimenez M, Gonzalez-Ballester D, Higuera JJ, Schwarz G, Galvan A, Fernandez E. Chlamydomonas reinhardtii CNX1E reconstitutes molybdenum cofactor biosynthesis in Escherichia coli mutants. Eukaryot. Cell 6: 1063-1067 (2007).
Lu G, Campbell WH, Schneider G, Lindqvist Y. Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 A resolution: relationship to other flavoprotein reductases. Structure 2: 809-821 (1994).
Lubitz SP, Weiner JH. The Escherichia coli ynfEFGHI operon encodes polypeptides which are paralogues of dimethyl sulfoxide reductase (DmsABC). Arch. Biochem. Biophys. 418: 205-216 (2003).
Lung SC, Leung A, Kuang R, Wang Y, Leung P, Lim BL. Phytase activity in tobacco (Nicotiana tabacum) root exudates is exhibited by a purple acid phosphatase. Phytochemistry 69: 365-373 (2008).
MacRae I, Segel IH. ATP sulfurylase from filamentous fungi: which sulfonucleotide is the true allosteric effector? Arch. Biochem. Biophys. 337: 17-26 (1997).
Magalon A, Asso M, Guigliarelli B, Rothery RA, Bertrand P, Giordano G, Blasco F. Molybdenum cofactor properties and [Fe-S] cluster coordination in Escherichia coli nitrate reductase A: investigation by site-directed mutagenesis of the conserved his-50 residue in the NarG subunit. Biochemistry 37: 7363-7370 (1998).
Marelja Z, Stocklein W, Nimtz M, Leimkuhler S. A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. J. Biol. Chem. 283: 25178-25185 (2008).
Marton L, Hrouda M, Pecsvaradi A, Czako M. T-DNA-insert-independent mutations induced in transformed plant cells during Agrobacterium co-cultivation. Transgenic Res. 3: 317-325 (1994).
McDevitt CA, Hanson GR, Noble CJ, Cheesman MR, McEwan AG. Characterization of the redox centers in dimethyl sulfide dehydrogenase from Rhodovulum sulfidophilum. Biochemistry 41: 15234-15244 (2002).
McNicholas PM, Gunsalus RP. The molybdate-responsive Escherichia coli ModE transcriptional regulator coordinates periplasmic nitrate reductase (napFDAGHBC) operon expression with nitrate and molybdate availability. J. Bacteriol. 184: 3253-3259 (2002).
Mendel RR. Biology of the molybdenum cofactor. J. Exp. Bot. 58: 2289-2296 (2007).
Mendel RR. Molybdenum cofactor of higher plants: biosynthesis and molecular biology. Planta 203: 399-405 (1997).
Mendel RR, Bittner F. Cell biology of molybdenum. Biochim. Biophys. Acta 1763: 621-635 (2006).
Mendel RR, Hansch R. Molybdoenzymes and molybdenum cofactor in plants. J. Exp. Bot. 53: 1689-1698 (2002).
Mendel RR, Schwarz G. Biosynthesis and molecular biology of the molybdenum cofactor (Moco). Met. Ions Biol. Syst. 39: 317-368 (2002).
Mertens JA, Shiraishi N, Campbell WH. Recombinant expression of molybdenum reductase fragments of plant nitrate reductase at high levels in Pichia pastoris. Plant Physiol. 123: 743-756 (2000).
Messerschmidt A, Niessen H, Abt D, Einsle O, Schink B, Kroneck PM. Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols. Proc. Natl. Acad. Sci. U.S.A. 101: 11571-11576 (2004).
Meyer C, Gonneau M, Caboche M, Rouze P. Identification by mutational analysis of four critical residues in the molybdenum cofactor domain of eukaryotic nitrate reductase. FEBS Lett. 370: 197-202 (1995).
Meyer O, Gremer L, Ferner R, Ferner M, Dobbek H, Gnida M, Meyer-Klaucke W, Huber R. The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase. Biol. Chem. 381: 865-876 (2000).
Milborrow BV. The pathway of biosynthesis of abscisic acid in vascular plants: a review of the present state of knowledge of ABA biosynthesis. J. Exp. Bot. 52: 1145-1164 (2001).
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).
Morozkina EV, Zvyagilskaya RA. Nitrate reductases: structure, functions, and effect of stress factors. Biochemistry (Mosc.) 72: 1151-1160 (2007).
Mouncey NJ, Mitchenall LA, Pau RN. Mutational analysis of genes of the mod locus involved in molybdenum transport, homeostasis, and processing in Azotobacter vinelandii. J. Bacteriol. 177: 5294-5302 (1995).
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).
Murillo M, Leustek T. ATP-sulfurylase from Arabidopsis thaliana and Escherichia coli are functionally equivalent but structurally and kinetically divergent: nucleotide sequence of two ATP-sulfurylase cDNAs from Arabidopsis thaliana and analysis of a recombinant enzyme. Arch. Biochem. Biophys. 323: 195-204 (1995).
Najmudin S, Gonzalez PJ, Trincao J, Coelho C, Mukhopadhyay A, Cerqueira NM, Romao CC, Moura I, Moura JJ, Brondino CD, Romao MJ. Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth coordination of the catalytic molybdenum. J. Biol. Inorg. Chem. 13: 737-753 (2008).
Nakamura T, Meyer C, Sano H. Molecular cloning and characterization of plant genes encoding novel peroxisomal molybdoenzymes of the sulphite oxidase family. J. Exp. Bot. 53: 1833-1836 (2002).
Nakano MM, Dailly YP, Zuber P, Clark DP. Characterization of anaerobic fermentative growth of Bacillus subtilis: identification of fermentation end products and genes required for growth. J. Bacteriol. 179: 6749-6755 (1997).
Navarro MT, Mariscal V, Macias MI, Fernandez E, Galvan A. Chlamydomonas reinhardtii strains expressing nitrate reductase under control of the cabII-1 promoter: isolation of chlorate resistant mutants and identification of new loci for nitrate assimilation. Photosynth. Res. 83: 151-161 (2005).
Neame PJ, Barber MJ. Conserved domains in molybdenum hydroxylases. The amino acid sequence of chicken hepatic sulfite oxidase. J. Biol. Chem. 264: 20894-20901 (1989).
Neubauer H, Pantel I, Gotz F. Characterization of moeB--part of the molybdenum cofactor biosynthesis gene cluster in Staphylococcus carnosus. FEMS Microbiol. Lett. 164: 55-62 (1998).
Noriega C, Hassett DJ, Rowe JJ. The mobA gene is required for assimilatory and respiratory nitrate reduction but not xanthine dehydrogenase activity in Pseudomonas aeruginosa. Curr. Microbiol. 51: 419-424 (2005).
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).
Okamoto PM, Garrett RH, Marzluf GA. Molecular characterization of conventional and new repeat-induced mutants of nit-3, the structural gene that encodes nitrate reductase in Neurospora crassa. Mol. Gen. Genet. 238: 81-90 (1993).
Okamoto PM, Marzluf GA. Nitrate reductase of Neurospora crassa: the functional role of individual amino acids in the heme domain as examined by site-directed mutagenesis. Mol. Gen. Genet. 240: 221-230 (1993).
Palmer T, Santini CL, Iobbi-Nivol C, Eaves DJ, Boxer DH, Giordano G. Involvement of the narJ and mob gene products in distinct steps in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli. Mol. Microbiol. 20: 875-884 (1996).
Palmer T, Vasishta A, Whitty PW, Boxer DH. Isolation of protein FA, a product of the mob locus required for molybdenum cofactor biosynthesis in Escherichia coli. Eur. J. Biochem. 222: 687-692 (1994).
Pantel I, Lindgren PE, Neubauer H, Gotz F. Identification and characterization of the Staphylococcus carnosus nitrate reductase operon. Mol. Gen. Genet. 259: 105-114 (1998).
Pau RN, Lawson DM. Transport, homeostasis, regulation, and binding of molybdate and tungstate to proteins. Met. Ions Biol. Syst. 39: 31-74 (2002).
Payne WJ, Liu MY, Bursakov SA, Le Gall J. Microbial and plant metabolism of NO. Biofactors 6: 47-52 (1997).
Peters F, Rother M, Boll M. Selenocysteine-containing proteins in anaerobic benzoate metabolism of Desulfococcus multivorans. J. Bacteriol. 186: 2156-2163 (2004).
Pierru B, Grosse S, Pignol D, Sabaty M. Genetic and biochemical evidence for the involvement of a molybdenum-dependent enzyme in one of the selenite reduction pathways of Rhodobacter sphaeroides f. sp. denitrificans IL106. Appl. Environ. Microbiol. 72: 3147-3153 (2006).
Pieterse CM, van't Klooster J, van den Berg-Velthuis GC, Govers F. NiaA, the structural nitrate reductase gene of Phytophthora infestans: isolation, characterization and expression analysis in Aspergillus nidulans. Curr. Genet. 27: 359-366 (1995).
Pignol D, Adriano JM, Fontecilla-Camps JC, Sabaty M. Crystallization and preliminary X-ray analysis of the periplasmic nitrate reductase (NapA-NapB complex) from Rhodobacter sphaeroides f. sp. denitrificans. Acta Crystallogr. D. Biol. Crystallogr. 57: 1900-1902 (2001).
Pilon M, Abdel-Ghany SE, Cohu CM, Gogolin KA, Ye H. Copper cofactor delivery in plant cells. Curr. Opin. Plant Biol. 9: 256-263 (2006).
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).
Pommier J, Mandrand MA, Holt SE, Boxer DH, Giordano G. A second phenazine methosulphate-linked formate dehydrogenase isoenzyme in Escherichia coli. Biochim. Biophys. Acta 1107: 305-313 (1992).
Porch TG, Tseung CW, Schmelz EA, Mark Settles A. The maize Viviparous10/Viviparous13 locus encodes the Cnx1 gene required for molybdenum cofactor biosynthesis. Plant J. 45: 250-263 (2006).
Pouteau S, Cherel I, Vaucheret H, Caboche M. Nitrate reductase mRNA regulation in Nicotiana plumbaginifolia nitrate reductase-deficient mutants. Plant Cell 1: 1111-1120 (1989).
Provan F, Aksland LM, Meyer C, Lillo C. Deletion of the nitrate reductase N-terminal domain still allows binding of 14-3-3 proteins but affects their inhibitory properties. Plant Physiol. 123: 757-764 (2000).
Ramaswamy KS, Endley S, Golden JW. Nitrate reductase activity and heterocyst suppression on nitrate in Anabaena sp. strain PCC 7120 require moeA. J. Bacteriol. 178: 3893-3898 (1996).
Rapson TD, Kappler U, Bernhardt PV. Direct catalytic electrochemistry of sulfite dehydrogenase: mechanistic insights and contrasts with related Mo enzymes. Biochim. Biophys. Acta 1777: 1319-1325 (2008).
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).
Rees DC. Great metalloclusters in enzymology. Annu. Rev. Biochem. 71: 221-246 (2002).
Reid RJ. Mechanisms of micronutrient uptake in plants. Aust. J. Plant Physiol. 28: 659-666 (2001).
Reyes F, Roldan MD, Klipp W, Castillo F, Moreno-Vivian C. Isolation of periplasmic nitrate reductase genes from Rhodobacter sphaeroides DSM 158: structural and functional differences among prokaryotic nitrate reductases. Mol. Microbiol. 19: 1307-1318 (1996).
Richardson DJ, Berks BC, Russell DA, Spiro S, Taylor CJ. Functional, biochemical and genetic diversity of prokaryotic nitrate reductases. Cell Mol. Life Sci. 58: 165-178 (2001).
Ridley H, Watts CA, Richardson DJ, Butler CS. Resolution of distinct membrane-bound enzymes from Enterobacter cloacae SLD1a-1 that are responsible for selective reduction of nitrate and selenate oxyanions. Appl. Environ. Microbiol. 72: 5173-5180 (2006).
Rieder C, Eisenreich W, O'Brien J, Richter G, Gotze E, Boyle P, Blanchard S, Bacher A, Simon H. Rearrangement reactions in the biosynthesis of molybdopterin--an NMR study with multiply 13C/15N labelled precursors. Eur. J. Biochem. 255: 24-36 (1998).
Rothery RA, Blasco F, Magalon A, Weiner JH. The diheme cytochrome b subunit (Narl) of Escherichia coli nitrate reductase A (NarGHI): structure, function, and interaction with quinols. J. Mol. Microbiol. Biotechnol. 3: 273-283 (2001).
Rothery RA, Magalon A, Giordano G, Guigliarelli B, Blasco F, Weiner JH. The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters. J. Biol. Chem. 273: 7462-7469 (1998).
Rubio LM, Flores E, Herrero A. Molybdopterin guanine dinucleotide cofactor in Synechococcus sp. nitrate reductase: identification of mobA and isolation of a putative moeB gene. FEBS Lett. 462: 358-362 (1999).
Rubio LM, Flores E, Herrero A. The narA locus of Synechococcus sp. strain PCC 7942 consists of a cluster of molybdopterin biosynthesis genes. J. Bacteriol. 180: 1200-1206 (1998).
Rubio LM, Flores E, Herrero A. Purification, cofactor analysis, and site-directed mutagenesis of Synechococcus ferredoxin-nitrate reductase. Photosynth. Res. 72: 13-26 (2002).
Rudolph MJ, Wuebbens MM, Rajagopalan KV, Schindelin H. Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation Nat. Struct. Biol. 8: 42-46 (2001).
Ruiz JM, Rivero RM, Romero L. Comparative effect of Al, Se, and Mo toxicity on NO3(-) assimilation in sunflower (Helianthus annuus L.) plants. J. Environ. Manage. 83: 207-212 (2007).
Sambasivarao D, Turner RJ, Bilous PT, Rothery RA, Shaw G, Weiner JH. Differential effects of a molybdopterin synthase sulfurylase (moeB) mutation on Escherichia coli molybdoenzyme maturation. Biochem. Cell Biol. 80: 435-443 (2002).
Sanchez DH, Lippold F, Redestig H, Hannah MA, Erban A, Kramer U, Kopka J, Udvardi MK. Integrative functional genomics of salt acclimatization in the model legume Lotus japonicus. Plant J. 53: 973-987 (2008).
Sandu C, Brandsch R. Functional analysis of the Escherichia coli molybdopterin cofactor biosynthesis protein MoeA by site-directed mutagenesis. Biol. Chem. 383: 319-323 (2002).
Sandu C, Brandsch R. Evidence for MoeA-dependent formation of the molybdenum cofactor from molybdate and molybdopterin in Escherichia coli. Arch. Microbiol. 178: 465-470 (2002).
Sanishvili R, Beasley S, Skarina T, Glesne D, Joachimiak A, Edwards A, Savchenko A. The crystal structure of Escherichia coli MoaB suggests a probable role in molybdenum cofactor synthesis. J. Biol. Chem. 279: 42139-42146 (2004).
Santini CL, Iobbi-Nivol C, Romane C, Boxer DH, Giordano G. Molybdoenzyme biosynthesis in Escherichia coli: in vitro activation of purified nitrate reductase from a chlB mutant. J. Bacteriol. 174: 7934-7940 (1992).
Sawers G. The hydrogenases and formate dehydrogenases of Escherichia coli. Antonie Van Leeuwenhoek 66: 57-88 (1994).
Schroder I, Wolin CD, Cavicchioli R, Gunsalus RP. Phosphorylation and dephosphorylation of the NarQ, NarX, and NarL proteins of the nitrate-dependent two-component regulatory system of Escherichia coli. J. Bacteriol. 176: 4985-4992 (1994).
Schwartz SH, Leon-Kloosterziel KM, Koornneef M, Zeevaart JA. Biochemical characterization of the aba2 and aba3 mutants in Arabidopsis thaliana. Plant Physiol. 114: 161-166 (1997).
Schwarz G, Boxer DH, Mendel RR. Molybdenum cofactor biosynthesis. The plant protein Cnx1 binds molybdopterin with high affinity. J. Biol. Chem. 272: 26811-26814 (1997).
Schwarz G, Mendel RR. Molybdenum cofactor biosynthesis and molybdenum enzymes. Annu. Rev. Plant Biol. 57: 623-647 (2006).
Schwarz G, Schulze J, Bittner F, Eilers T, Kuper J, Bollmann G, Nerlich A, Brinkmann H, Mendel RR. The molybdenum cofactor biosynthetic protein Cnx1 complements molybdate-repairable mutants, transfers molybdenum to the metal binding pterin, and is associated with the cytoskeleton. Plant Cell 12: 2455-2472 (2000).
Sekowska A, Kung HF, Danchin A. Sulfur metabolism in Escherichia coli and related bacteria: facts and fiction. J. Mol. Microbiol. Biotechnol. 2: 145-177 (2000).
Self WT, Grunden AM, Hasona A, Shanmugam KT. Transcriptional regulation of molybdoenzyme synthesis in Escherichia coli in response to molybdenum: ModE-molybdate, a repressor of the modABCD (molybdate transport) operon is a secondary transcriptional activator for the hyc and nar operons. Microbiology 145: 41-55 (1999).
Siddiqui RA, Warnecke-Eberz U, Hengsberger A, Schneider B, Kostka S, Friedrich B. Structure and function of a periplasmic nitrate reductase in Alcaligenes eutrophus H16. J. Bacteriol. 175: 5867-5876 (1993).
Simonovic AD, Gaddameedhi S, Anderson MD. In-gel precipitation of enzymatically released phosphate. Anal. Biochem. 334: 312-317 (2004).
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).
Skipper L, Campbell WH, Mertens JA, Lowe DJ. Pre-steady-state kinetic analysis of recombinant Arabidopsis NADH:nitrate reductase: rate-limiting processes in catalysis. J. Biol. Chem. 276: 26995-27002 (2001).
Stadtman TC. Discoveries of vitamin B12 and selenium enzymes. Annu. Rev. Biochem. 71: 1-16 (2002).
Stevenson CE, Sargent F, Buchanan G, Palmer T, Lawson DM. Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution. Structure Fold. Des. 8: 1115-1125 (2000).
Stewart V, Bledsoe PJ, Williams SB. Dual overlapping promoters control napF (periplasmic nitrate reductase) operon expression in Escherichia coli K-12. J. Bacteriol. 185: 5862-5870 (2003).
Stolz JF, Basu P. Evolution of nitrate reductase: molecular and structural variations on a common function. Chembiochem. 3: 198-206 (2002).
Su W, Huber SC, Crawford NM. Identification in vitro of a post-translational regulatory site in the hinge 1 region of Arabidopsis nitrate reductase. Plant Cell 8: 519-527 (1996).
Su W, Mertens JA, Kanamaru K, Campbell WH, Crawford NM. Analysis of wild-type and mutant plant nitrate reductase expressed in the methylotrophic yeast Pichia pastoris. Plant Physiol. 115: 1135-1143 (1997).
Suzuki M, Mark Settles A, Tseung CW, Li QB, Latshaw S, Wu S, Porch TG, Schmelz EA, James MG, McCarty DR. The maize viviparous15 locus encodes the molybdopterin synthase small subunit. Plant J. 45: 264-274 (2006).
Taoka A, Yoshimatsu K, Kanemori M, Fukumori Y. Nitrate reductase from the magnetotactic bacterium Magnetospirillum magnetotacticum MS-1: purification and sequence analyses. Can. J. Microbiol. 49: 197-206 (2003).
Taylor NJ, Cowan AK. Xanthine dehydrogenase and aldehyde oxidase impact plant hormone homeostasis and affect fruit size in 'Hass' avocado. J. Plant Res. 117: 121-130 (2004).
Tejada-Jimenez M, Llamas A, Sanz-Luque E, Galvan A, Fernandez E. A high-affinity molybdate transporter in eukaryotes. Proc. Natl. Acad. Sci. U.S.A. 104: 20126-20130 (2007).
Temple CA, Rajagopalan KV. Mechanism of assembly of the bis(molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase. J. Biol. Chem. 275: 40202-40210 (2000).
Terao M, Kurosaki M, Saltini G, Demontis S, Marini M, Salmona M, Garattini E. Cloning of the cDNAs coding for two novel molybdo-flavoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase. J. Biol. Chem. 275: 30690-30700 (2000).
Thapper A, Behrens A, Fryxelius J, Johansson MH, Prestopino F, Czaun M, Rehder D, Nordlander E. Synthesis and characterization of molybdenum oxo complexes of two tripodal ligands: reactivity studies of a functional model for molybdenum oxotransferases. Dalton Trans. 21: 3566-3571 (2005).
Thiel T, Pratte B, Zahalak M. Transport of molybdate in the cyanobacterium Anabaena variabilis ATCC 29413. Arch. Microbiol. 179: 50-56 (2002).
Thomas G, Potter L, Cole JA. The periplasmic nitrate reductase from Escherichia coli: a heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site. FEMS Microbiol. Lett. 174: 167-171 (1999).
Tischner R, Planchet E, Kaiser WM. Mitochondrial electron transport as a source for nitric oxide in the unicellular green alga Chlorella sorokiniana. FEBS Lett. 576: 151-155 (2004).
Truong HN, Meyer C, Daniel-Vedele F. Characteristics of Nicotiana tabacum nitrate reductase protein produced in Saccharomyces cerevisiae. Biochem. J. 278: 393-397 (1991).
Turner WL, Plaxton WC. Purification and characterization of banana fruit acid phosphatase. Planta 214: 243-249 (2001).
Uchimura H, Enjoji H, Seki T, Taguchi A, Takaya N, Shoun H. Nitrate reductase-formate dehydrogenase couple involved in the fungal denitrification by Fusarium oxysporum. J. Biochem. 131: 579-586 (2002).
Unkles SE, Campbell EI, Punt PJ, Hawker KL, Contreras R, Hawkins AR, Van den Hondel CA, Kinghorn JR. The Aspergillus niger niaD gene encoding nitrate reductase: upstream nucleotide and amino acid sequence comparisons. Gene 111: 149-155 (1992).
Unkles SE, Heck IS, Appleyard MV, Kinghorn JR. Eukaryotic molybdopterin synthase. Biochemical and molecular studies of Aspergillus nidulans cnxG and cnxH mutants. J. Biol. Chem. 274: 19286-19293 (1999).
Unkles SE, Smith J, Kanan GJ, Millar LJ, Heck IS, Boxer DH, Kinghorn JR. The Aspergillus nidulans cnxABC locus is a single gene encoding two catalytic domains required for synthesis of precursor Z, an intermediate in molybdenum cofactor biosynthesis. J. Biol. Chem. 272: 28381-28390 (1997).
Vaucheret H, Vincentz M, Kronenberger J, Caboche M, Rouze P. Molecular cloning and characterisation of the two homologous genes coding for nitrate reductase in tobacco. Mol. Gen. Genet. 216: 10-15 (1989).
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).
Vergnes A, Pommier J, Toci R, Blasco F, Giordano G, Magalon A. NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly. J. Biol. Chem. 281: 2170-2176 (2006).
Wagner UG, Stupperich E, Kratky C. Structure of the molybdate/tungstate binding protein Mop from Sporomusa ovata. Structure Fold. Des. 8: 1127-1136 (2000).
Walkenhorst HM, Hemschemeier SK, Eichenlaub R. Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia coli and modR, a regulatory gene. Microbiol. Res. 150: 347-361 (1995).
Wang W, Zhang W, Lu J, Yang Y, Chiao J, Zhao G, Jiang W. MoeA, an enzyme in the molybdopterin synthesis pathway, is required for rifamycin SV production in Amycolatopsis mediterranei U32. Appl. Microbiol. Biotechnol. 60: 139-146 (2002).
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).
Watts CA, Ridley H, Dridge EJ, Leaver JT, Reilly AJ, Richardson DJ, Butler CS. Microbial reduction of selenate and nitrate: common themes and variations. Biochem. Soc. Trans. 33: 173-175 (2005).
Weare WW, Dai X, Byrnes MJ, Chin JM, Schrock RR, Muller P. Catalytic reduction of dinitrogen to ammonia at a single molybdenum center. Proc. Natl. Acad. Sci. U.S.A. 103: 17099-17106 (2006).
Whitehead MP, Gurr SJ, Grieve C, Unkles SE, Spence D, Ramsden M, Kinghorn JR. Homologous transformation of Cephalosporium acremonium with the nitrate reductase-encoding gene (niaD). Gene 90: 193-198 (1990).
Wilkinson JQ, Crawford NM. Identification and characterization of a chlorate-resistant mutant of Arabidopsis thaliana with mutations in both nitrate reductase structural genes NIA1 and NIA2. Mol. Gen. Genet. 239: 289-297 (1993).
Williams RS, Davis MA, Howlett BJ. Nitrate reductase of the ascomycetous fungus, Leptosphaeria maculans: gene sequence and chromosomal location. Mol. Gen. Genet. 244: 1-8 (1994).
Witte CP, Igeno MI, Mendel R, Schwarz G, Fernandez E. The Chlamydomonas reinhardtii MoCo carrier protein is multimeric and stabilizes molybdopterin cofactor in a molybdate charged form. FEBS Lett. 431: 205-209 (1998).
Wollers S, Heidenreich T, Zarepour M, Zachmann D, Kraft C, Zhao Y, Mendel RR, Bittner F. Binding of sulfurated molybdenum cofactor to the C-terminal domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration. J. Biol. Chem. 283: 9642-9650 (2008).
Wu Q, Knowles R. Cellular regulation of nitrate uptake in denitrifying Flexibacter canadensis. Can. J. Microbiol. 40: 576-582 (1994).
Wuebbens MM, Liu MT, Rajagopalan K, Schindelin H. Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC. Structure Fold. Des. 8: 709-718 (2000).
Xiong L, Ishitani M, Lee H, Zhu JK. The Arabidopsis los5/aba3 locus encodes a molybdenum cofactor sulfurase and modulates cold stress- and osmotic stress-responsive gene expression. Plant Cell 13: 2063-2083 (2001).
Xu YC, Zhao BL. The main origin of endogenous NO in higher non-leguminous plants. Plant Physiol. Biochem. 41: 833-838 (2003).
Yandulov DV, Schrock RR. Catalytic reduction of dinitrogen to ammonia at a single molybdenum center. Science 301: 76-78 (2003).
Yang SH, Berberich T, Miyazaki A, Sano H, Kusano T. Ntdin, a tobacco senescence-associated gene, is involved in molybdenum cofactor biosynthesis. Plant Cell Physiol. 44: 1037-1044 (2003).
Yanni YG, Rizk RY, Abd El-Fattah FK, Squartini A, Corich V, Giacomini A, de Bruijn F, Rademaker J, Maya-Flores J, Ostrom P, Vega-Hernandez M, Hollingsworth RI, Martinez-Molina E, Mateos P, Velazquez E, Wopereis J, Triplett E, Umali-Garcia M, et al. The beneficial plant growth-promoting association of Rhizobium leguminosarum bv. trifolii with rice roots. Aust. J. Plant Physiol. 28: 845-870 (2001).
Yesbergenova Z, Yang G, Oron E, Soffer D, Fluhr R, Sagi M. The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have distinct reactive oxygen species signatures and are induced by drought and abscisic acid. Plant J. 42: 862-876 (2005).
Yoshimatsu K, Iwasaki T, Fujiwara T. Sequence and electron paramagnetic resonance analyses of nitrate reductase NarGH from a denitrifying halophilic euryarchaeote Haloarcula marismortui. FEBS Lett. 516: 145-150 (2002).
Zahalak M, Pratte B, Werth KJ, Thiel T. Molybdate transport and its effect on nitrogen utilization in the cyanobacterium Anabaena variabilis ATCC 29413. Mol. Microbiol. 51: 539-549 (2004).
Zdunek-Zastocka E. Molecular cloning, characterization and expression analysis of three aldehyde oxidase genes from Pisum sativum L. Plant Physiol. Biochem. 46: 19-28 (2008).
Zdunek-Zastocka E, Lips HS. Plant molybdoenzymes and their response to stress. Acta Physiol. Plant. 25: 437-452 (2003).
Zeiler KG, Solomonson LP. Regulation of Chlorella nitrate reductase: control of enzyme activity and immunoreactive protein levels by ammonia. Arch. Biochem. Biophys. 269: 46-54 (1989).
Zhao D, Curatti L, Rubio LM. Evidence for nifU and nifS participation in the biosynthesis of the iron-molybdenum cofactor of nitrogenase. J. Biol. Chem. 282: 37016-37025 (2007).
Zimmer W, Mendel R. Molybdenum metabolism in plants. Plant Biol. 1: 160-168 (1999).
Number of references = 301
| PubMed Search | Entrez Protein Search | ISI Web of Knowledge Search | Scirus Search |
|