Abaibou H, Pommier J, Benoit S, Giordano G, Mandrand-Berthelot MA. Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase. J. Bacteriol. 177: 7141-7149 (1995).

Akinterinwa O, Khankal R, Cirino PC. Metabolic engineering for bioproduction of sugar alcohols. Curr. Opin. Biotechnol. 19: 461-467 (2008).

Ambard-Bretteville F, Sorin C, Rebeille F, Hourton-Cabassa C, Colas des Francs-Small C. Repression of formate dehydrogenase in Solanum tuberosum increases steady-state levels of formate and accelerates the accumulation of proline in response to osmotic stress. Plant Mol. Biol. 52: 1153-1168 (2003).

Andersen HW, Pedersen MB, Hammer K, Jensen PR. Lactate dehydrogenase has no control on lactate production but has a strong negative control on formate production in Lactococcus lactis. Eur. J. Biochem. 268: 6379-6389 (2001).

Asanuma N, Iwamoto M, Hino T. Structure and transcriptional regulation of the gene encoding pyruvate formate-lyase of a ruminal bacterium, Streptococcus bovis. Microbiology 145: 151-157 (1999).

Barber RD, Donohue TJ. Function of a glutathione-dependent formaldehyde dehydrogenase in Rhodobacter sphaeroides formaldehyde oxidation and assimilation. Biochemistry 37: 530-537 (1998).

Berg BL, Stewart V. Structural genes for nitrate-inducible formate dehydrogenase in Escherichia coli K-12. Genetics 125: 691-702 (1990).

Berrios-Rivera SJ, Bennett GN, San KY. The effect of increasing NADH availability on the redistribution of metabolic fluxes in Escherichia coli chemostat cultures. Metab. Eng. 4: 230-237 (2002).

Berrios-Rivera SJ, Bennett GN, San KY. Metabolic engineering of Escherichia coli: increase of NADH availability by overexpressing an NAD(+)-dependent formate dehydrogenase. Metab. Eng. 4: 217-229 (2002).

Berrios-Rivera SJ, San KY, Bennett GN. The effect of NAPRTase overexpression on the total levels of NAD, the NADH/NAD+ ratio, and the distribution of metabolites in Escherichia coli. Metab. Eng. 4: 238-247 (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).

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).

Castillo RM, Mizuguchi K, Dhanaraj V, Albert A, Blundell TL, Murzin AG. A six-stranded double-psi beta barrel is shared by several protein superfamilies. Structure Fold. Des. 7: 227-236 (1999).

Cole J. Nitrate reduction to ammonia by enteric bacteria: redundancy, or a strategy for survival during oxygen starvation? FEMS Microbiol. Lett. 136: 1-11 (1996).

Collakova E, Goyer A, Naponelli V, Krassovskaya I, Gregory JF 3rd, Hanson AD, Shachar-Hill Y. Arabidopsis 10-formyl tetrahydrofolate deformylases are essential for photorespiration. Plant Cell 20: 1818-1832 (2008).

Collins LA, Egan SM, Stewart V. Mutational analysis reveals functional similarity between NARX, a nitrate sensor in Escherichia coli K-12, and the methyl-accepting chemotaxis proteins. J. Bacteriol. 174: 3667-3675 (1992).

Cramm R. Genomic view of energy metabolism in Ralstonia eutropha H16. J. Mol. Microbiol. Biotechnol. 16: 38-52 (2009).

Cruz JA, Emery C, Wust M, Kramer DM, Lange BM. Metabolite profiling of Calvin cycle intermediates by HPLC-MS using mixed-mode stationary phases. Plant J. 55: 1047-1060 (2008).

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).

Deutch CE. Oxidation of L-thiazolidine-4-carboxylate by L-proline dehydrogenase in Escherichia coli. J. Gen. Microbiol. 138: 1593-1598 (1992).

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).

Durnin G, Clomburg J, Yeates Z, Alvarez PJ, Zygourakis K, Campbell P, Gonzalez R. Understanding and harnessing the microaerobic metabolism of glycerol in Escherichia coli. Biotechnol. Bioeng. 103: 148-161 (2009).

Egan SM, Stewart V. Nitrate regulation of anaerobic respiratory gene expression in narX deletion mutants of Escherichia coli K-12. J. Bacteriol. 172: 5020-5029 (1990).

Egorov AM, Tishkov VI, Avilova TV, Popov VO. S-Formyl glutathione as a substrate of bacterial formate dehydrogenase. Biochem. Biophys. Res. Commun. 104: 1-5 (1982).

Even S, Garrigues C, Loubiere P, Lindley ND, Cocaign-Bousquet M. Pyruvate metabolism in Lactococcus lactis is dependent upon glyceraldehyde-3-phosphate dehydrogenase activity. Metab. Eng. 1: 198-205 (1999).

Even S, Lindley ND, Cocaign-Bousquet M. Molecular physiology of sugar catabolism in Lactococcus lactis IL1403. J. Bacteriol. 183: 3817-3824 (2001).

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

Findrik Z, Vasic-Racki D. Biotransformation of D-methionine into L-methionine in the cascade of four enzymes. Biotechnol. Bioeng. 98: 956-967 (2007).

Garrigues C, Goupil-Feuillerat N, Cocaign-Bousquet M, Renault P, Lindley ND, Loubiere P. Glucose metabolism and regulation of glycolysis in Lactococcus lactis strains with decreased lactate dehydrogenase activity. Metab. Eng. 3: 211-217 (2001).

Garrigues C, Mercade M, Cocaign-Bousquet M, Lindley ND, Loubiere P. Regulation of pyruvate metabolism in Lactococcus lactis depends on the imbalance between catabolism and anabolism. Biotechnol. Bioeng. 74: 108-115 (2001).

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).

Gokarn RR, Eiteman MA, Altman E. Metabolic analysis of Escherichia coli in the presence and absence of the carboxylating enzymes phosphoenolpyruvate carboxylase and pyruvate carboxylase. Appl. Environ. Microbiol. 66: 1844-1850 (2000).

Goldberg JD, Yoshida T, Brick P. Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 A resolution. J. Mol. Biol. 236: 1123-1140 (1994).

Gouesbet G, Abaibou H, Wu LF, Mandrand-Berthelot MA, Blanco C. Osmotic repression of anaerobic metabolic systems in Escherichia coli. J. Bacteriol. 175: 214-221 (1993).

Goyer A, Johnson TL, Olsen LJ, Collakova E, Shachar-Hill Y, Rhodes D, Hanson AD. Characterization and metabolic function of a peroxisomal sarcosine and pipecolate oxidase from Arabidopsis. J. Biol. Chem. 279: 16947-16953 (2004).

Grabbe R, Schmitz RA. Oxygen control of nif gene expression in Klebsiella pneumoniae depends on NifL reduction at the cytoplasmic membrane by electrons derived from the reduced quinone pool. Eur. J. Biochem. 270: 1555-1566 (2003).

Gross R, Pisa R, Sanger M, Lancaster CRD, Simon J. Characterization of the menaquinone reduction site in the diheme cytochrome b membrane anchor of Wolinella succinogenes NiFe-hydrogenase. J. Biol. Chem. 279: 274-281 (2004).

Hemschemeier S, Grund M, Keuntje B, Eichenlaub R. Isolation of Escherichia coli mutants defective in uptake of molybdate. J. Bacteriol. 173: 6499-6506 (1991).

Herbik A, Giritch A, Horstmann C, Becker R, Balzer HJ, Baumlein H, Stephan UW. Iron and copper nutrition-dependent changes in protein expression in a tomato wild type and the nicotianamine-free mutant chloronerva. Plant Physiol. 111: 533-540 (1996).

Hourton-Cabassa C, Ambard-Bretteville F, Moreau F, Davy de Virville J, Remy R, Francs-Small CC. Stress induction of mitochondrial formate dehydrogenase in potato leaves. Plant Physiol. 116: 627-635 (1998).

Iwami Y, Takahashi-Abbe S, Takahashi N, Abbe K, Yamada T. Rate-limiting steps of glucose and sorbitol metabolism in Streptococcus mutans cells exposed to air. Oral. Microbiol. Immunol. 15: 325-328 (2000).

Jormakka M, Byrne B, Iwata S. Formate dehydrogenase - a versatile enzyme in changing environments. Curr. Opin. Struct. Biol. 13: 418-423 (2003).

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).

Krebs HA, Hems R, Tyler B. The regulation of folate and methionine metabolism. Biochem. J. 158: 341-353 (1976).

Kreuzwieser J, Schnitzler JP, Steinbrecher R. Biosynthesis of organic compounds emitted by plants. Plant Biol. 1: 149-159 (1999).

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).

Laville J, Blumer C, Von Schroetter C, Gaia V, Defago G, Keel C, Haas D. Characterization of the hcnABC gene cluster encoding hydrogen cyanide synthase and anaerobic regulation by ANR in the strictly aerobic biocontrol agent Pseudomonas fluorescens CHA0. J. Bacteriol. 180: 3187-3196 (1998).

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).

Li R, Moore M, King J. Investigating the regulation of one-carbon metabolism in Arabidopsis thaliana. Plant Cell Physiol. 44: 233-241 (2003).

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).

Maidan NN, Gonchar MV, Sibirny AA. Oxidation of exogenous formaldehyde in methylotrophic and nonmethylotrophic yeast cells. Biochemistry (Mosc.) 62: 636-640 (1997).

McKenzie KQ, Jones EW. Mutants of formyltetrahydrofolate interconversion pathway of Saccharomyces cerevisiae. Genetics 86: 85-102 (1977).

McKinlay JB, Shachar-Hill Y, Zeikus JG, Vieille C. Determining Actinobacillus succinogenes metabolic pathways and fluxes by NMR and GC-MS analyses of 13C-labeled metabolic product isotopomers. Metab. Eng. 9: 177-192 (2007).

Menzel K, Ahrens K, Zeng A, Deckwer W. Kinetic, dynamic, and pathway studies of glycerol metabolism by Klebsiella pneumoniae in anaerobic continuous culture: IV. Enzymes and fluxes of pyruvate metabolism. Biotechnol. Bioeng. 60: 617-626 (1998).

Meyer M, Granderath K, Andreesen JR. Purification and characterization of protein PB of betaine reductase and its relationship to the corresponding proteins glycine reductase and sarcosine reductase from Eubacterium acidaminophilum. Eur. J. Biochem. 234: 184-191 (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).

Nakagawa T, Ito T, Fujimura S, Chikui M, Mizumura T, Miyaji T, Yurimoto H, Kato N, Sakai Y, Tomizuka N. Molecular characterization of the glutathione-dependent formaldehyde dehydrogenase gene FLD1 from the methylotrophic yeast Pichia methanolica. Yeast 21: 445-453 (2004).

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).

Nakano MM, Zuber P. Anaerobic growth of a "strict aerobe". Annu. Rev. Microbiol. 52: 165-190 (1998).

Nour JM, Rabinowitz JC. Isolation, characterization, and structural organization of 10-formyltetrahydrofolate synthetase from spinach leaves. J. Biol. Chem. 266: 18363-18369 (1991).

Pasternack LB, Laude DA Jr, Appling DR. Whole-cell detection by 13C NMR of metabolic flux through the C1-tetrahydrofolate synthase/serine hydroxymethyltransferase enzyme system and effect of antifolate exposure in Saccharomyces cerevisiae. Biochemistry 33: 7166-7173 (1994).

Pasternack LB, Littlepage LE, Laude DA Jr, Appling DR. 13C NMR analysis of the use of alternative donors to the tetrahydrofolate-dependent one-carbon pools in Saccharomyces cerevisiae. Arch. Biochem. Biophys. 326: 158-165 (1996).

Peters F, Rother M, Boll M. Selenocysteine-containing proteins in anaerobic benzoate metabolism of Desulfococcus multivorans. J. Bacteriol. 186: 2156-2163 (2004).

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).

Pomper BK, Saurel O, Milon A, Vorholt JA. Generation of formate by the formyltransferase/hydrolase complex (Fhc) from Methylobacterium extorquens AM1. FEBS Lett. 523: 133-137 (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).

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).

Rojkova AM, Galkin AG, Kulakova LB, Serov AE, Savitsky PA, Fedorchuk VV, Tishkov VI. Bacterial formate dehydrogenase. Increasing the enzyme thermal stability by hydrophobization of alpha-helices. FEBS Lett. 445: 183-188 (1999).

Sanghani PC, Stone CL, Ray BD, Pindel EV, Hurley TD, Bosron WF. Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase. Biochemistry 39: 10720-10729 (2000).

Sawers G. The hydrogenases and formate dehydrogenases of Escherichia coli. Antonie Van Leeuwenhoek 66: 57-88 (1994).

Sawers G, Watson G. A glycyl radical solution: oxygen-dependent interconversion of pyruvate formate-lyase. Mol. Microbiol. 29: 945-54 (1998).

Shams Yazdani S, Gonzalez R. Engineering Escherichia coli for the efficient conversion of glycerol to ethanol and co-products. Metab. Eng. 10: 340-351 (2008).

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).

Simon J. Enzymology and bioenergetics of respiratory nitrite ammonification. FEMS Microbiol. Rev. 26: 285-309 (2002).

Simon J, Gross R, Einsle O, Kroneck PM, Kroger A, Klimmek O. A NapC/NirT-type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes. Mol. Microbiol. 35: 686-696 (2000).

Stadtman TC. Selenocysteine. Annu. Rev. Biochem. 65: 83-100 (1996).

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).

Suzuki K, Itai R, Suzuki K, Nakanishi H, Nishizawa NK, Yoshimura E, Mori S. Formate dehydrogenase, an enzyme of anaerobic metabolism, is induced by iron deficiency in barley roots. Plant Physiol. 116: 725-732 (1998).

Takahashi N, Yamada T. Pathways for amino acid metabolism by Prevotella intermedia and Prevotella nigrescens. Oral Microbiol. Immunol. 15: 96-102 (2000).

Thompson P, Bowsher CG, Tobin AK. Heterogeneity of mitochondrial protein biogenesis during primary leaf development in barley. Plant Physiol. 118: 1089-1099 (1998).

Tishkov VI, Galkin AG, Fedorchuk VV, Savitsky PA, Rojkova AM, Gieren H, Kula MR. Pilot scale production and isolation of recombinant NAD+- and NADP+-specific formate dehydrogenases. Biotechnol. Bioeng. 64: 187-193 (1999).

Tsou AY, Ransom SC, Gerlt JA, Buechter DD, Babbitt PC, Kenyon GL. Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli. Biochemistry 29: 9856-9862 (1990).

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).

Uotila L, Koivusalo M. Purification of formaldehyde and formate dehydrogenases from pea seeds by affinity chromatography and S-formylglutathione as the intermediate of formaldehyde metabolism. Arch. Biochem. Biophys. 196: 33-45 (1979).

Vadas AJ, Schroder I, Monbouquette HG. Room-temperature synthesis of L-alanine using the alanine dehydrogenase of the hyperthermophilic archaeon Archaeoglobus fulgidus. Biotechnol. Prog. 18: 909-911 (2002).

van der Maarel MJ, Jansen M, Haanstra R, Meijer WG, Hansen TA. Demethylation of dimethylsulfoniopropionate to 3-S-methylmercaptopropionate by marine sulfate-reducing bacteria. Appl. Environ. Microbiol. 62: 3978-3984 (1996).

West MG, Horne DW, Appling DR. Metabolic role of cytoplasmic isozymes of 5,10-methylenetetrahydrofolate dehydrogenase in Saccharomyces cerevisiae. Biochemistry 35: 3122-3132 (1996).

Wood HG. Life with CO or CO2 and H2 as a source of carbon and energy. FASEB J. 5: 156-163 (1991).

Yang YT, Bennett GN, San KY. Effect of inactivation of nuo and ackA-pta on redistribution of metabolic fluxes in Escherichia coli. Biotechnol. Bioeng. 65: 291-297 (1999).

Yang YT, Bennett GN, San KY. The effects of feed and intracellular pyruvate levels on the redistribution of metabolic fluxes in Escherichia coli. Metab. Eng. 3: 115-123 (2001).

Yang YT, San KY, Bennett GN. Redistribution of metabolic fluxes in Escherichia coli with fermentative lactate dehydrogenase overexpression and deletion. Metab. Eng. 1: 141-152 (1999).

Zhu J, Shimizu K. Effect of a single-gene knockout on the metabolic regulation in Escherichia coli for D-lactate production under microaerobic condition. Metab. Eng. 7: 104-115 (2005).

Zhu Y, Eiteman MA, Altman R, Altman E. High glycolytic flux improves pyruvate production by metabolically engineered Escherichia coli. Appl. Environ. Microbiol. 74: 6649-6655 (2008).

Number of references = 95