A unified scheme for carbon and electron flow coupled to ATP synthesis by substrate‐level phosphorylation in the methanogenic bacteria

Lancaster, Jack R.

doi:10.1016/0014-5793(86)81214-5

Cited by 35 publications

(11 citation statements)

References 52 publications

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“…Since ATP synthesis in M. voltae is not diminished under conditions in which the transmembrane electrical potential is collapsed by the addition of the protononophore SF6847, substrate-level phosphorylation has been proposed as the physiological mechanism of ATP synthesis (10,25 The most thoroughly studied E1E2 ATPases have been those of the plasma membranes of fungal, plant, and animal cells. Although reports of E1E2 ATPases in procaryotes have been limited to Streptococcus faecalis (17,19), E. coli (18), and Acholeplasma laidlawii (22), it is likely that their distribution is more widespread.…”

Section: Resultsmentioning

confidence: 99%

“…The inability of the ionophore to reach the internal membranes in whole cells has been proposed to explain this difference in sensitivity. On the basis of evidence that electron transfer-driven ATP synthesis in Methanococcus voltae is not dependent on a proton electrochemical gradient, a molecular scheme in which ATP synthesis is coupled directly to electron transfer has been proposed (10,25). Furthermore, the M. voltae ATPase is not considered to function physiologically as an ATP synthase; rather, it is believed to be involved in electrogenic sodium translocation (1,8).…”

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confidence: 99%

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Identification of a vanadate-sensitive, membrane-bound ATPase in the archaebacterium Methanococcus voltae

Dharmavaram¹,

Konisky²

1987

J Bacteriol

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Identification of a vanadate-sensitive, membrane-bound ATPase in the archaebacterium Methanococcus voltae

Dharmavaram¹,

Konisky²

1987

J Bacteriol

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“…The relatively low levels of formate dehydrogenase activity in acetate-and methanol-grown cells could potentially function to provide formyl groups for cell carbon synthesis, as recently proposed for Methanobacterium thermoautotrophicum (22a). Other possibilities for the high levels of formyltransferase include cycling of a formyl group in the hypothetical mechanism proposed for substratelevel phosphorylation in methanogens (14).…”

Section: Methodsmentioning

confidence: 99%

Protein content and enzyme activities in methanol- and acetate-grown Methanosarcina thermophila

et al. 1990

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The cell extract protein content of acetate-and methanol-grown Methanosarcina thermophila TM-1 was examined by two-dimensional polyacrylamide gel electrophoresis. More than 100 mutually exclusive spots were present in acetate-and methanol-grown cells. Spots corresponding to acetate kinase, phosphotransacetylase, and the five subunits of the carbon monoxide dehydrogenase complex were identified in acetate-grown cells. Activities of formylmethanofuran dehydrogenase, formylmethanofuran:tetrahydromethanopterin formyltransferase, 5,10-methenyltetrahydromethanopterin cyclohydrolase, methylene tetrahydromethanopterin:coenzyme F420 oxidoreductase, formate dehydrogenase, and carbonic anhydrase were examined in acetate-and methanol-grown Methanosarcina thermnophila. Levels of formyltransferase in either acetate-or methanol-grown Methanosarcina thermophila were approximately half the levels detected in H2-CO2-grown Methanobacterium thermoautotrophicum. All other enzyme activities were significantly lower in acetate-and methanol-grown Methanosarcina thermophila.Of the known methanogens, Methanosarcina species are the most catabolically diverse and are therefore amenable to the study of catabolite influence on protein synthesis. Methanosarcina thermophila TM-1 is capable of using acetate, methanol, or methylated amines as growth substrates (28). Except for the reductive demethylation of methyl coenzyme M, the pathways for utilization of acetate or methanol by the methanogenic archaeobacteria (see Fig. 3) (23, 25) are distinct from the pathway for reduction of carbon dioxide (20). When acetate is used, acetate kinase and phosphotransacetylase catalyze the activation of acetate to acetyl coenzyme A prior to the proposed cleavage of the carbon-carbon bond by the carbon monoxide dehydrogenase (CODH) complex (23). The levels of these enzymes are severalfold greater in acetate-grown cells than they are in methanol-grown cells (1,15,23). Electrons for the demethylation of methyl coenzyme M derive from the oxidation of methanol (see reaction 5 in Fig. 3) or the carbonyl group of acetate (see reaction 2 in Fig. 3). The presence of formylmethanofuran dehydrogenase activity in extracts of methanol-grown Methanosarcina barkeri is consistent with the proposal that methanol is oxidized by a reversal of the carbon dioxide reduction pathway (5). Growth of Methanosarcina thermophila TM-1 is supported by acetate or methanol, but the organism reduces carbon dioxide to methane only after an extended adaptation period, and growth is poor (28). Here we present results of two-dimensional (2-D) gel electrophoretic analyses of whole-cell proteins which estimate the extent of regulation by the growth substrate and report the activities of the enzymes that catalyze one-carbon redox reactions in extracts of acetate-and methanol-grown cells.

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“…In the methanogenic bacteria, sodium has been implicated in several cellular functions, including growth [2], methane formation [2-41, electron transfer [4], amino acid transport [51, pH homeostasis [6,7], and membrane potential-induced ATP synthesis [8,91. We have recently presented evidence for a role for sodium as a coupling ion in Methanococcus voltae for internal ion and solute homeostasis (powered by an electrogenic sodium-translocating ATPase), with cellular ATP production coupled to electron transfer by a separate, direct mechanism [9][10][11][12]. The experimental evidence includes ATP synthesis driven by electrogenic movement of sodium + Present address: Department of Radiation Oncology, University of Arizona Health Sciences Center, Tucson, AZ 85724, USA * To whom correspondence should be addressed through a membrane-bound ATPase and uncoupler-insensitive ATP synthesis coupled to electron transfer.…”

Section: Introductionmentioning

confidence: 99%

Discrimination between transmembrane ion gradient‐driven and electron transfer‐driven ATP synthesis in the methanogenic bacteria

Al-Mahrouq¹,

Carper²,

Lancaster³

1986

FEBS Letters

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As with Methanococcus voltae [(1986) FEBS Lett. 200, 177-180], ATP synthesis in Methanobacterium thermoautotrophicum (AH) can be driven by the imposition of a sodium gradient, but only in the presence of a counterion. Monensin (but not SF6847) inhibits this synthesis. Methanogenic electron transfer-driven ATP synthesis, however, is insensitive to the combination of these two ionophores. In M. voltae, 117 I~M diethylstilbestrol effectively inhibits both membrane potential-and sodium gradient-driven ATP synthesis, but has no effect on ATP production coupled to methanogenesis. In Mb, thermoautotrophicurn (AII), a similar pattern of inhibition is exhibited by harmaline, an inhibitor of sodium-linked membrane transport systems. We conclude that ATP-driven sodium translocation and electron transfer-driven ATP synthesis are accomplished by separate entities, at least for these two only distantly related species ot methanogen. MethanogenBioenergetics Na + pump A TPase

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A unified scheme for carbon and electron flow coupled to ATP synthesis by substrate‐level phosphorylation in the methanogenic bacteria

Cited by 35 publications

References 52 publications

Identification of a vanadate-sensitive, membrane-bound ATPase in the archaebacterium Methanococcus voltae

Identification of a vanadate-sensitive, membrane-bound ATPase in the archaebacterium Methanococcus voltae

Protein content and enzyme activities in methanol- and acetate-grown Methanosarcina thermophila

Discrimination between transmembrane ion gradient‐driven and electron transfer‐driven ATP synthesis in the methanogenic bacteria

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