The tungsten-containing formate dehydrogenase from Methylobacterium extorquens AM1: Purification and properties

European Journal of Biochemistry

Volumn 270, Issue 2, 2003, Pages 325-333

  Laukel, Markus ^a,b   Chistoserdova, Ludmila ^c   Lidstrom, Mary E ^c,d   Vorholt, Julia A ^b  

^a MAX PLANCK INSTITUTE FOR TERRESTRIAL MICROBIOLOGY   (Germany)

^b CNRS   (France)

^c University of Washington   (United States)

^d UNIVERSITY OF WASHINGTON   (United States)

Author keywords

Formate dehydrogenase; Methylotrophic bacteria; Molybdenum; One carbon (C1) metabolism; Tungsten

Indexed keywords

DIMER; FLAVINE MONONUCLEOTIDE; FORMATE DEHYDROGENASE; HYBRID PROTEIN; IRON DERIVATIVE; ISOENZYME; MOLYBDOPTERIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SELENOCYSTEINE; SULFUR; TUNGSTEN;

ALPHA CHAIN; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL GENE; BETA CHAIN; CARBOXY TERMINAL SEQUENCE; CHROMOSOME; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME ISOLATION; ENZYME PURIFICATION; ENZYME SUBUNIT; EUBACTERIUM; GENE IDENTIFICATION; METHYLOBACTERIUM EXTORQUENS; MOORELLA THERMOACETICA; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; FORMATE DEHYDROGENASES; METHYLOBACTERIUM EXTORQUENS; MOLECULAR SEQUENCE DATA; MOLYBDENUM; NAD; SEQUENCE ANALYSIS, PROTEIN; SPECTROPHOTOMETRY; TUNGSTEN; TUNGSTEN COMPOUNDS;

BACTERIA (MICROORGANISMS); CLOSTRIDIUM; EUBACTERIUM ACIDAMINOPHILUM; METHYLOBACTERIUM; METHYLOBACTERIUM EXTORQUENS; MOORELLA; MOORELLA THERMOACETICA; NEGIBACTERIA; PROTEOBACTERIA; UNCULTURED ALPHA PROTEOBACTERIUM;

EID: 0037240872     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03391.x     Document Type: Article

References (46)

1. Vorholt, J.A. (2002) Cofactor-dependent pathways of formaldehyde oxidation in methylotrophic bacteria. Arch. Microbiol. 178, 239-249.
2. Pomper, B.K., Saurel, O., Milon, A. & Vorholt, J.A. (2002) Generation of formate by the formyltransferase/hydrolase complex (fhc) from Methylobacterium extorquens AM1. FEBS Lett. 523, 133-137.
3. 1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic archaea. Science 281, 99-102.
4. Vorholt, J.A., Chistoserdova, L., Lidstrom, M.E. & Thauer, R.K. (1998) The NADP-dependent methylene tetrahydromethanopterin dehydrogenase in Methylobacterium extorquens AM1. J. Bacteriol. 180, 5351-5356.
5. Pomper, B.K., Vorholt, J.A., Chistoserdova, L., Lidstrom, M.E. & Thauer, R.K. (1999) A methenyl tetrahydromethanopterin cyclohydrolase and a methenyl tetrahydrofolate cyclohydrolase in Methylobacterium extorquens AM1. Eur. J. Biochem. 261, 475-480.
6. 1 metabolism. Biochem. J. 350, 609-629.
7. Hagemeier, C.H., Chistoserdova, L., Lidstrom, M.E., Thauer, R.K. & Vorholt, J.A. (2000) Characterization of a second methylene tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1. Eur. J. Biochem. 267, 3762-3769.
8. Vorholt, J.A., Marx, C.J., Lidstrom, M.E. & Thauer, R.K. (2000) Novel formaldehyde-activating enzyme in Methylobacterium extorquens AM1 required for growth on methanol. J. Bacteriol. 182, 6645-6650.
9. Thauer, R.K. (1998) Biochemistry of methanogenesis: a tribute to Marjory Stephenson. Microbiology 144, 2377-2406.
10. Pomper, B.K. & Vorholt, J.A. (2001) Characterization of the formyltransferase from Methylobacterium extorquens AM1. Eur. J. Biochem. 269, 4769-4775.
11. 1 compounds. 6. Oxidation of methanol, formaldehyde and formate by methanol-grown Pseudomonas AM1. Biochem. J. 93, 281-290.
12. 1 metabolism. In Molybdenum and Tungsten. Their Roles in Biological Processes (Sigel, A. & Sigel, H., eds), pp. 571-619. M. Dekker, Inc., New York, USA.
13. +-dependent formate dehydrogenase in Pseudomonas sp. 101 cells grown on a molybdenum-containing medium. FEMS Microbiol. Lett. 60, 197-200.
14. +-dependent formate dehydrogenases in the facultative methylotroph Mycobacterium vaccae 10. FEMS Microbiol. Lett. 81, 95-100.
15. Lamzin, V.S., Dauter, Z., Popov, V.O., Harutyunyan, E.H. & Wilson, K.S. (1994) High resolution structures of holo and apo formate dehydrogenase. J. Mol. Biol. 236, 759-785.
16. 313 pair in enzyme catalysis. FEBS Lett. 390, 104-108.
17. Asano, Y., Sekigawa, T., Inukai, H. & Nakazawa, A. (1988) Purification and properties of formate dehydrogenase from Moraxella sp. strain C-1. J. Bacteriol. 170, 3189-3193.
18. Yoch, D.C., Chen, Y.-P. & Hardin, M.G. (1990) Formate dehydrogenase from the methane oxidizer Methylosinus trichosporium OB3b. J. Bacteriol. 172, 4456-4463.
19. Jollie, D.R. & Lipscomb, J.D. (1991) Formate dehydrogenase from Methylosinus trichosporium OB3b. Purification and spectroscopic characterization of the cofactors. J. Biol. Chem. 266, 21853-21863.
20. Girio, F.M., Amaral-Collaco, M.T. & Attwood, M. (1994) The effect of molybdate and tungstate ions on the metabolic rates and enzyme activities in methanol-grown Methylobacterium sp. RXM. Appl. Microbiol. Biotechnol. 40, 898-903.
21. Duarte, R.O., Reis, A.R., Girio, F., Moura, I., Moura, J.J.G. & Collaco, T.A. (1997) The formate dehydrogenase isolated from the aerobe Methylobacterium sp. RXM is a molybdenum-containing protein. Biochem. Biophys. Res. Com. 230, 30-34.
22. Kletzin, A. & Adams, M.W.W. (1996) Tungsten in biological systems. FEMS Microbiol. Rev. 18, 5-63.
23. Ljungdahl, L.G. & Andreesen, J.R. (1975) Tungsten, a component of active formate dehydrogenase from Clostridium thermo-aceticum. FEBS Lett. 54, 279-282.
24. Yamamoto, I., Saiki, T., Liu, S.-M. & Ljungdahl, L.G. (1983) Purification and properties of NADP-dependent formate dehydrogenase from Clostridium thermoaceticum, a tungsten-selenium-iron protein. J. Biol. Chem. 258, 1826-1832.
25. Fulton, G.L., Nunn, D.N. & Lidstrom, M.E. (1984) Molecular cloning of a malyl coenzyme A lyase gene from Pseudomonas sp. strain AM1, a facultative methylotroph. J. Bacteriol. 160, 718-723.
26. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
27. Fish, W.W. (1988) Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples. Methods Enzymol. 158, 357-364.
28. Hedderich, R., Berkessel, A. & Thauer, R.K. (1990) Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg). Eur. J. Biochem. 193, 255-261.
29. Heim, S., Künkel, A., Thauer, R.K. & Hedderich, R. (1998) Thiol: Fumarate reductase (Tfr) from Methanobacterium thermoautotrophicum. Identification of the catalytic sites for fumarate reduction and thiol oxidation. Eur. J. Biochem. 253, 292-299.
30. +-linked formate dehydrogenase of Ralstonia eutropha. J. Biol. Chem. 273, 26349-26360.
31. Bokranz, M., Gutmann, M., Kortner, C., Kojro, E., Fahrenholz, F., Lauterbach, F. & Kröger, A. (1991) Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes. Arch. Microbiol. 156, 119-128.
32. Graentzdoerffer, A. (2000) Formiat-Stoffwechsel in Eubacterium acidaminophilum: Molekulare und biochemische Charakterisie-rung der Wolfram- und Selen-haltigen Formiat-Dehydrogenasen sowie einer Eisen-Hydrogenase. Dissertation, Martin-Luther-Universität, Halle-Wittenberg, Germany.
33. Zinoni, F., Birkman, A., Stadtman, T.C. & Böck, A. (1986) Nucleotide sequence and expression of the selenocysteine-containing popypeptide of formate dehydrogenase (formate-hydrogenlyase-linked) from Escherichia coli. Proc. Natl. Acad. Sci. USA 83, 4650-4654.
34. 4 cluster. Science 275, 1305-1308.
35. Appel, J. & Schulz, R. (1996) Sequence analysis of an operon of a NAD(P)-reducing nickel hydrogenase from the cyanobacterium Synechocystis sp. PCC 6803 gives additional evidence for direct coupling of the enzyme to NAD(P)H-dehydrogenase (complex I). Biochim. Biophys. Acta 1298, 141-147.
36. Schmitz, O., Boison, G., Hilscher, R., Hundeshagen, B., Zimmer, W., Lottspeich, F. & Bothe, H. (1995) Molecular biological analysis of a bidirectional hydrogenase from cyanobacteria. Eur. J. Biochem. 233, 266-276.
37. Deckert, G., Warren, P.V., Gaasterland, T., Young, W.G., Lenox, A.L., Graham, D.E., Overbeek, R., Snead, M.A., Keller, M., Aujay, M., Huber, R., Feldman, R.A., Short, J.M., Olsen, G.J. & Swanson, R.V. (1998) The complete genome of the hyperthermophilic bacterium Aquifex aeolicus. Nature 392, 353-358.
38. Boison, G., Schmitz, O., Schmitz, B. & Bothe, H. (1998) Unusual gene arrangement of the bidirectional hydrogenase and functional analysis of its diaphorase subunit HoxU in respiration of the unicellular cyanobacterium Anacystis nidulans. Curr. Microbiol. 36, 253-258.
39. Blanchard, J.S. & Cleland, W.W. (1980) Kinetic and chemical mechanisms of yeast formate dehydrogenase. Biochemistry 19, 3543-3550.
40. Friedebold, J. & Bowien, B. (1993) Physiological and biochemical characterization of the soluble formate dehydrogenase, a molybdoenzyme from Alcaligenes eutrophus. J. Bacteriol. 175, 4719-4728.
41. 2 oxidoreductase from Clostridium pasteurianum, a molybdenum iron-sulfur-protein. Eur. J. Biochem. 85, 125-135.
42. Hille, R., Rétey, J., Bartlewski-Hof, U., Reichenbecher, W. & Schink, B. (1999) Mechanistic aspects of molybdenum-containing enzymes. FEMS Microbiol. Rev. 22, 489-501.
43. Ferry, J.G. (1990) Formate dehydrogenase. FEMS Microbiol. Rev. 87, 377-382.
44. Burgdorf, T., Bömmer, D. & Bowien, B. (2001) Involvement of an unusual mol operon in molybdopterin cofactor biosynthesis in Ralstonia eutropha. J. Mol. Microbiol. Biotechnol. 3, 619-629.
45. Makdessi, K., Andreesen, J.R. & Pich, A. (2001) Tungstate uptake by a highly specific ABC transporter in Eubacterium acidaminophilum. J. Biol. Chem. 276, 24557-24564.
46. Zindel, U., Freudenberg, W., Reith, M., Andreesen, J.R., Schnell, J. & Widdel, F. (1988) Eubacterium acidaminophilum new species. A versatile amino acid-degrading anaerobe producing or utilizing hydrogen or formate. Description and enzymatic studies. Arch. Microbiol. 150, 254-266.