Composition of the major elements and trace elements of 10 methanogenic bacteria determined by inductively coupled plasma emission spectrometry

Scherer, Paul; Lippert, H.; Wolff, G.

doi:10.1007/bf02916619

Cited by 167 publications

(90 citation statements)

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“…However, the cellular zinc content of of methanogens is higher in the species that utili2 and zinc concentrations are positively correlate molybdenum content of the formate-utilizing species (29 …”

Section: Discussionmentioning

confidence: 90%

Composition of the coenzyme F420-dependent formate dehydrogenase from Methanobacterium formicicum

Schauer¹,

Ferry²

1986

J Bacteriol

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The coenzyme F420-dependent formate dehydrogenase from Methanobacterium formicicum was purified to electrophoretic homogeneity by anoxic procedures which included the addition o(f azide, flavin adenine dinucleotide (FAD), glycerol, and 2-mercaptoethanol to all buffer solutions to stabilize iictivity. The enzyme contains, in approximate miolar ratios, 1 FAD molecule and 1 molybdenum, 2 zinc, 21 to 24 iron, and 25 to 29 inorganic sulfur atoms. Denaturation of the enzyme released a molybdopterin cofactor. The enzyme has a molecular weight of 177,000 and consists of one each of two different subunits, giving the composition olol.The molecular weight of the a-subunit is 85,000, and that of the ,-subunit is 53,000. The UV-visible spectrum is typical of nonheme iron-sulfur flavoprotein. Reduction of the enzyme facilitated dissociation of FAD, and the FAD-depleted enzyme was unable to reduce coenzyme F420. Preincubation of the FAD-depleted enzyme with FAD restored coenzyme F420-dependent activity.The methanogenic bacteria are phylogenetically distant from eubacteria and eucaryotes (10). Consistent with this division, they utilize several unusual cofactors, including the low-potential electron carrier coenzyme F420 (8-hydroxy-5-deazaflavin) (6). Several oxidation and reduction reactions are linked to coenzyme F420, including the oxidation of formate catalyzed by formate dehydrogenase, which supplies electrons for the reduction of carbon dioxide to methane (8,16,27,30).Spectroscopic studies of the formate dehydrogenase from Methanobacterium formicicum indicate the presence of molybdenum and iron-sulfur centers (1). Present methods for the purification of this enzyme result in a decrease in the rate of coenzyme F420 reduction relative to methyl viologen reduction (27, 28), but preincubation with flavin adenine dihucleotide (FAD) restores coenzyme F420-dependent activity, sUggesting that FAD is an essential component (28). Studies have also identified a fluorescent pterin compound associated with the enzyme (27; H. D. May, N. L. Schauer, and J. G. Ferry, submitted for publication). The quantitation of components in coenzyme F420-dependent enzymes is necessary to further understand their function in intramolecular electron transfer. Here we report on the composition and physical properties of the formate dehydrogenase from M. formicicum purified to electrophoretic homogeneity by methods that preserve coenzyme F420-dependent activity.MATERIALS AND METHODS Cell material. M. formicicum JF1 (DSM 2639) was grown in 12-liter batches as described previously (26), except that the basal medium contained the following constituents (grams per liter): NaHCO2, 6.0; NH4Cl, 1.48; K2HPO4, 1.36; KH2PO4, 0.90; NaCl, 0.45; MgSO4, 0.045; CaCl2 * 2H20, 0.06; NaCH3CO2, 2.0; Na2CO3, 3.0; Na2MoO4, 0.024; cysteine hydrochloride, 0.27; Na2SeO3, 0.0002; Na2S -9H20, 0.27; Fe(NH4)(SO4)2, 0.06; and resazurin, 0.001. Cultures were sparged with H2-CO2 (4:1) at 300 ml/min. * Corresponding author. t Present address: Department of Microbiology, University of ...

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Section: Discussionmentioning

confidence: 90%

Composition of the coenzyme F420-dependent formate dehydrogenase from Methanobacterium formicicum

Schauer¹,

Ferry²

1986

J Bacteriol

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“…Zinc is often adventitiously bound during purification of proteins. However, zinc is present at high concentrations (50 to 630 ppm) in methanogens (34) and has been found in formate dehydrogenase (33) and F420-non-reactive hydrogenase (1) of M. formicicum. Selenium was not found in the enzyme from M. formicicum and has only been reported present in the F420-hydrogenases from M. vannielii (41) and M. voltae (27).…”

Section: Discussionmentioning

confidence: 99%

Purification and properties of the membrane-associated coenzyme F420-reducing hydrogenase from Methanobacterium formicicum

Baron

Ferry

1989

J Bacteriol

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The membrane-associated coenzyme F420-reducing hydrogenase of Methanobacterium formicicum was purified 87-fold to electrophoretic homogeneity. The enzyme contained a, I, and fy subunits (molecular weights of 43,600, 36,700, and 28,800, respectively) and formed aggregates (molecular weight, 1,020,000) of a coenzyme F420-active a4,1yz, trimer (molecular weight, 109,000). The hydrogenase contained 1 mol of flavin adenine dinucleotide (FAD), 1 mol of nickel, 12 to 14 mol of iron, and 11 mol of acid-labile sulfide per mol of the 109,000-molecular-weight species, but no selenium. The isoelectric point was 5.6. The amino acid sequence I-N3-P-N2-R-N,-EGH-N6-V (where N is any amino acid) was conserved in the N-termini of the a subunits of the F420-hydrogenases from M. formicicum and Methanobacterium thermoautotrophicum and of the largest subunits of nickel-containing hydrogenases from Desulfovibrio baculatus, Desulfovibrio gigas, and Rhodobacter capsulatus. The purified F420-hydrogenase required reductive reactivation before assay. FAD dissociated from the enzyme during reactivation unless potassium salts were present, yielding deflavoenzyme that was unable to reduce coenzyme F420. Maximal coenzyme F420-reducing activity was obtained at 55°C and pH 7.0 to 7.5, and with 0.2 to 0.8 M KCI in the reaction mixture. The enzyme catalyzed H2 production at a rate threefold lower than that for H2 uptake and reduced coenzyme F420, methyl viologen, flavins, and 7,8-didemethyl-8-hydroxy-5-deazariboflavin. Specific antiserum inhibited the coenzyme F420-dependent but not the methyl viologen-dependent activity of the purified enzyme.

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“…As in Fe concentrations, in the concentrations of Ni, Co and W an increase was measured due to the additives in the present study. In a previous study with 10 species of methanogens, the composition of them was observed to vary quite a bit (Scherer et al 1983). Methanogens were seen to consist of C (37-44 % WW), H (5.5-6.5 %), N (9.5-12.8 %), Na (0.3-4.0 %), K (0.13-5.0 %), S (0.56-1.2 %), P (0.5-2.8 %), Ca (85-4500 ppm), Mg (0.09-0.53 %), Fe (0.07-0.28 %), Ni (65-180 ppm), Co (10-120 ppm), Mo (10-70 ppm), Zn (50-630 ppm), Cu (<10-160 ppm), and Mn (<5-25 ppm, Scherer et al 1983).…”

Section: Additives To Improve Anaerobic Digestion Of Pig Slaughterhoumentioning

confidence: 97%

Screening pretreatment methods to enhance thermophilic anaerobic digestion of pulp and paper mill wastewater treatment secondary sludge

Bayr

Kaparaju

Rintala

2013

Chemical Engineering Journal

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Esitetään Jyväskylän yliopiston matemaattis-luonnontieteellisen tiedekunnan suostumuksella julkisesti tarkastettavaksi yliopiston Ylistönrinteellä, salissa YAA303 toukokuun 23. päivänä 2014 kello 12.Academic dissertation to be publicly discussed, In this thesis, the anaerobic digestion of industrial by-products from meat and pulp and paper industry were studied. These materials, which are treated mainly like wastes, were seen to be potential substrates for anaerobic digestion. Methane yields of ca. 700 dm 3 kg volatile solids (VS)added -1 were obtained for slaughterhouse wastes, alone and in co-digestion with rendering wastes. On the other hand, methane yields of 190-240 dm 3 kgVSadded -1 were obtained in the monodigestion of pulp and paper industry primary sludge, and 150-170 dm 3 kgVSadded -1 in the co-digestion of primary sludge with secondary sludge. In the digestion of slaughterhouse and rendering wastes, mesophilic conditions were more stable, and the feasible organic loading rates (OLRs) were 1-1.5 kgVS m -3 d -1 and hydraulic retention times (HRTs) were 50 d. For pulp and paper mill wastewater sludge, thermophilic conditions were more stable with the feasible OLRs of 1-2 kgVS m -3 d -1 and the HRTs of 14-32 d. The digestion processes of these industrial by-products can easily turn unstable. In the digestion of slaughterhouse and rendering wastes, process imbalance may occur due to inhibition from intermediate products like volatile fatty acids, long-chain fatty acids and ammonia. On the contrary, in the digestion of pulp and paper mill wastewater sludge, the low nitrogen content and low pH may cause problems. It was observed that the more stable digestion process of slaughterhouse waste is achieved by additive of Co, Ni, Se, W, Fe and HCl. In addition, in pulp and paper mill secondary sludge digestion, hydrothermal pretreatment, among the studied 12 single or combined pre-treatments, increased the methane yield by 19-31 %. In conclusion, the digestion of two different kinds of industrial by-products was seen to be feasible, although operational conditions should be optimised and possibly enhancement methods used to ensure the stable digestion processes of these vulnerable organic materials.

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Composition of the major elements and trace elements of 10 methanogenic bacteria determined by inductively coupled plasma emission spectrometry

Cited by 167 publications

References 33 publications

Composition of the coenzyme F420-dependent formate dehydrogenase from Methanobacterium formicicum

Composition of the coenzyme F420-dependent formate dehydrogenase from Methanobacterium formicicum

Purification and properties of the membrane-associated coenzyme F420-reducing hydrogenase from Methanobacterium formicicum

Screening pretreatment methods to enhance thermophilic anaerobic digestion of pulp and paper mill wastewater treatment secondary sludge

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