Abstract
Cell extracts of Methanosarcina barkeri grown on methanol in media supplemented with molybdate exhibited a specific activity of formylmethanofuran dehydrogenase of approximately 1 U (1 μmol/min)/mg protein. When the growth medium was supplemented with tungstate rather than with molybdate, the specific activity was only 0.04 U/mg. Despite this reduction in specific activity growth on methanol was not inhibited. An inhibition of both growth and synthesis of active formylmethanofuran dehydrogenase was observed, however, when H2 and CO2 were the energy substrates. The results indicate that, in contrast to Methanobacterium wolfei and Methanobacterium thermoautotrophicum, M. barkeri possesses only a molybdenum containing formylmethanofuran dehydrogenase and not in addition a tungsten isoenzyme.
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References
Adams MWW (1993) Enzymes and proteins from organisms that grow near and above 100°C. Annu Rev Microbiol 47:627–658
Bertram PA, Schmitz RA, Linder D, Thauer RK (1994) Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum: identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase. Arch Microbiol 161: 220–228
Bradford MM (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
Ferry JG (1993) Methanogenesis. Chapman & Hall, New York
Fraústo da Silva JJR, Williams RJP (1991) The biological chemistry of the elements: the inorganic chemistry of life. Clarendon Press, Oxford, pp 411–435
Karrasch M, Bott M, Thauer RK (1989) Carbonic anhydrase activity in acetate grown Methanosarcina barkeri. Arch Microbiol 151:137–142
Karrasch M, Börner G, Enßle M, Thauer RK (1990) The molybdoenzyme formylmethanofuran dehydrogenase from Methanosarcina barkeri contains a pterin cofactor. Eur J Biochem 194:367–372
Leonhardt U, Andreesen JR (1977) Some properties of formate dehydrogenase, accumulation and incorporation of 185W-tungsten into proteins of Clostridium formicoaceticum. Arch Microbiol 115:277–284
Mukund S, Adams MWW, (1990) Characterization of tungsteniron-sulfur protein exhibiting novel spectroscopic and redox properties from the hyperthermophilic archaebacterium Pyrococcus furiosus. J Biol Chem 265:11508–11516
Mukund S, Adams MWW (1991) The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase: evidence for its participation in a unique glycolytic pathway. J Biol Chem 266:14208–14216
Mukund S, Adams MWW (1993) Characterization of a novel tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon, Themococcus litoralis: a role for tungsten in peptide catabolism. J Biol Chem 268: 13592–13600
Schmitz R, Richter M, Linder D, Thauer RK (1992) A tungsten-containing active formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei. Eur J Biochem 207:559–565
Stetter KO (1993) Life at the upper temperature border. In: Trân Than Vân JK, Mounolou JC, Schneider J, McKay C (eds) Colloque Interdisciplinaire du Comité National de la Recherche Scientifique, Frontiers of Life. Editions Frontières, Gif-sur-Yvette, pp 195–219
White H, Simon H (1992) The role of tungstate and/or molybdate in the formation of aldehyde oxidoreductase in Clostridium thermoaceticum and other acetogens; immunological distances of such enzymes. Arch Microbiol 158:81–84
White H, Strobl G, Feicht R, Simon H (1989) Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to aldehydes. Eur J Biochem 184: 89–96
White H, Feicht R, Huber C, Lottspeich F, Simon H (1991) Purification and some properties of the tungsten-containing carboxylic acid reductase from Clostridium formicoaceticum. Biol Chem Hoppe-Seyler 372:999–1005
Yamamoto I, Saiki T, Liu SM, Ljungdahl LG (1983) Purification and properties of NADP-dependent formate dehydrogenase from Clostridium thermoaceticum, a tungsten-selenium-iron protein. J Biol Chem 258:1826–1832
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Schmitz, R.A., Bertram, P.A. & Thauer, R.K. Tungstate does not support synthesis of active formylmethanofuran dehydrogenase in Methanosarcina barkeri . Arch. Microbiol. 161, 528–530 (1994). https://doi.org/10.1007/BF00307775
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DOI: https://doi.org/10.1007/BF00307775