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Chapter 13 : Acetate-Based Methane Production
Author:
James G. Ferry1
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Affiliations:
1: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802
Content Type: Monograph
Publication Year:
2008
Category: Applied and Industrial Microbiology
Book DOI:
10.1128/9781555815547
Chapter DOI:
10.1128/9781555815547.ch13
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Abstract:
This chapter explores the microbiology and biochemistry of acetate conversion to methane, a key component of biomethanation. It provides a fundamental background appropriate for stimulating advances to improve the process that will ensure biomethanation among the competitive alternatives to fossil fuels. Biomethanation of organic matter in nature occurs in diverse habitats such as freshwater sediments, rice paddies, sewage digesters, the rumen, the lower intestinal tract of monogastric animals, landfills, hydrothermal vents, coastal marine sediments, and the subsurface. Methanosarcina species synthesize tetrahydrosarcinapterin (H4SPT) which serves the same function as tetrahydromethanopterin (H4MPT). The aceticlastic and CO2 reduction pathways generate primary sodium and proton gradients that are the only possible driving forces for ATP synthesis. The production of acetate from complex biomass by fermentative and acetogenic anaerobes and the subsequent conversion of acetate to methane by aceticlastic methanogens are of primary importance in the biomethanation process. Aceticlastic methanogenesis is the major factor controlling the rate and reliability of the process; thus, a comprehensive understanding of these methanogens is paramount for developing an efficient process for biomethanation of renewable and waste biomass for use as a biofuel. Although the enzymology of reactions leading from acetate to methane by Methanosarcina species is fairly well understood, there have been only a few investigations reported on the mechanism of energy conservation and regulation of gene expression. Further, global proteomic and microarray analyses have identified a host of proteins and genes in Methanosarcina species, many with unknown functions, that may be important or essential.
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
Figures
Acetate-Based Methane Production
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Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13fig01
Figure 1
The global carbon cycle in nature. (A) Fixation of CO2 into organic matter; (B) aerobic decomposition of organic matter to CO2; (C) anaerobic decomposition of organic matter to fermentative end products; (D) anaerobic conversion of fermentative end products to methane and escape into aerobic environments; (E) aerobic oxidation of methane to CO2 by O2-requiring methylotrophs.
10.1128/9781555815547/f0156-01_thmb.gif
10.1128/9781555815547/f0156-01.gif
Figure 1
The global carbon cycle in nature. (A) Fixation of CO2 into organic matter; (B) aerobic decomposition of organic matter to CO2; (C) anaerobic decomposition of organic matter to fermentative end products; (D) anaerobic conversion of fermentative end products to methane and escape into aerobic environments; (E) aerobic oxidation of methane to CO2 by O2-requiring methylotrophs.
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13fig02
Figure 2.
Methane-producing freshwater consortia.
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Figure 2.
Methane-producing freshwater consortia.
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13fig03
Figure 3.
Phase-contrast micrographs of Methanosarcina mazei showing cells in pseudosarcinal aggregates (left) and single cells (right). Bars, 10 μm. Reprinted from Applied and Environmental Microbiology (
Sowers et al., 1993
) with permission of the publisher.
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10.1128/9781555815547/f0157-01.gif
Figure 3.
Phase-contrast micrographs of Methanosarcina mazei showing cells in pseudosarcinal aggregates (left) and single cells (right). Bars, 10 μm. Reprinted from Applied and Environmental Microbiology ( Sowers et al., 1993 ) with permission of the publisher.
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13fig04
Figure 4.
Thin-section electron micrograph of Methanosarcina thermophila showing a cell aggregate enclosed by an outer membrane. Bar, 1 μm. Reprinted from International Journal of Systematic Bacteriology (
Zinder et al., 1985
) with permission of the publisher.
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Figure 4.
Thin-section electron micrograph of Methanosarcina thermophila showing a cell aggregate enclosed by an outer membrane. Bar, 1 μm. Reprinted from International Journal of Systematic Bacteriology ( Zinder et al., 1985 ) with permission of the publisher.
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13fig05
Figure 5.
Scanning electron micrograph of Methanosaeta concilii strain T-3 filaments. Reprinted from Bioscience, Biotechnology, and Biochemistry (
Mizukami et al., 2006
) with permission of the publisher.
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Figure 5.
Scanning electron micrograph of Methanosaeta concilii strain T-3 filaments. Reprinted from Bioscience, Biotechnology, and Biochemistry ( Mizukami et al., 2006 ) with permission of the publisher.
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13fig06
Figure 6.
Thin section of “Methanothrix” (Methanosaeta) concilii. Spacer plugs are indicated by arrows, and “M” indicates the amorphous granular layer. Bar, 1 μm. Reprinted from Canadian Journal of Microbiology (
Beveridge et al., 1986
) with permission of the publisher.
10.1128/9781555815547/f0158-01_thmb.gif
10.1128/9781555815547/f0158-01.gif
Figure 6.
Thin section of “Methanothrix” (Methanosaeta) concilii. Spacer plugs are indicated by arrows, and “M” indicates the amorphous granular layer. Bar, 1 μm. Reprinted from Canadian Journal of Microbiology ( Beveridge et al., 1986 ) with permission of the publisher.
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13equ01
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Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13equ02
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Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13equ03
Untitled
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Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13equ04
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Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13fig07
Figure 2.
Cofactors and coenzymes utilized in the pathway for aceticlastic methanogenesis.
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Figure 2.
Cofactors and coenzymes utilized in the pathway for aceticlastic methanogenesis.
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13equ05
Untitled
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Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13equ06
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Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13equ07
Untitled
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Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13fig08
Figure 8.
Overview of the aceticlastic and CO2 reduction pathways. H4M(S)PT, tetrahydromethanopterin (H4MPT) or tetrahydrosarcinapterin (H4SPT); CoM, coenzyme M; CoB, coenzyme B.
10.1128/9781555815547/f0159-01_thmb.gif
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Figure 8.
Overview of the aceticlastic and CO2 reduction pathways. H4M(S)PT, tetrahydromethanopterin (H4MPT) or tetrahydrosarcinapterin (H4SPT); CoM, coenzyme M; CoB, coenzyme B.
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13fig09
Figure 9.
Proposed mechanism of sodium translocation by the methyl-H4M(S)PT:coenzyme M methyltransferase. Reprinted from Biochimica et Biophysica Acta (
Gottschalk and Thauer, 2001
) with permission of the publisher.
10.1128/9781555815547/f0160-01_thmb.gif
10.1128/9781555815547/f0160-01.gif
Figure 9.
Proposed mechanism of sodium translocation by the methyl-H4M(S)PT:coenzyme M methyltransferase. Reprinted from Biochimica et Biophysica Acta ( Gottschalk and Thauer, 2001 ) with permission of the publisher.
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13fig10
Figure 10.
Mechanism proposed for methyl-coenzyme M methylreductase. Adapted from Ermler et al., 1997.
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10.1128/9781555815547/f0161-01.gif
Figure 10.
Mechanism proposed for methyl-coenzyme M methylreductase. Adapted from Ermler et al., 1997.
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13equ08
Untitled
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Untitled
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13equ09
Untitled
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Untitled
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13equ10
Untitled
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Untitled
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13fig11
Figure 11.
Pathways for conversion of acetate to methane by M. mazei (A) and M. acetivorans (B). Ack, acetate kinase; Pta, phosphotransacetylase; CoA-SH, coenzyme A; H4SPT, tetrahydrosarcinapterin; Fdr, reduced ferredoxin; Fdo, oxidized ferredoxin; Cdh, CO dehydrogenase/acetyl-CoA synthase; CoM-SH, coenzyme M; Mtr, methyl-H4SPT:CoM-SH methyltransferase; CoB-SH, coenzyme B; Cam, carbonic anhydrase; Ech, H2-evolving hydrogenase; Vho, H2-consuming hydrogenase; Ma-Rnf, M. acetivorans Rnf; MP, methanophenazine; Hdr-DE, heterodisulfide reductase; Mrp, multiple resistance/pH regulation Na+ /H antiporter; Atp, H -translocating A1A0 ATP synthase. Adapted from Li et al., 2006.
10.1128/9781555815547/f0162-01_thmb.gif
10.1128/9781555815547/f0162-01.gif
Figure 11.
Pathways for conversion of acetate to methane by M. mazei (A) and M. acetivorans (B). Ack, acetate kinase; Pta, phosphotransacetylase; CoA-SH, coenzyme A; H4SPT, tetrahydrosarcinapterin; Fdr, reduced ferredoxin; Fdo, oxidized ferredoxin; Cdh, CO dehydrogenase/acetyl-CoA synthase; CoM-SH, coenzyme M; Mtr, methyl-H4SPT:CoM-SH methyltransferase; CoB-SH, coenzyme B; Cam, carbonic anhydrase; Ech, H2-evolving hydrogenase; Vho, H2-consuming hydrogenase; Ma-Rnf, M. acetivorans Rnf; MP, methanophenazine; Hdr-DE, heterodisulfide reductase; Mrp, multiple resistance/pH regulation Na+ /H antiporter; Atp, H -translocating A1A0 ATP synthase. Adapted from Li et al., 2006.
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13equ11
Untitled
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Untitled
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13fig12
Figure 12.
The A cluster of Acs from Moorella thermoacetica. Reprinted from Critical Reviews in Biochemistry and Molecular Biology (
Ragsdale, 2004
) with permission of the publisher.
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10.1128/9781555815547/f0164-01.gif
Figure 12.
The A cluster of Acs from Moorella thermoacetica. Reprinted from Critical Reviews in Biochemistry and Molecular Biology ( Ragsdale, 2004 ) with permission of the publisher.
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
/content/10.1128/9781555815547.ch13.ch13equ12
Untitled
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10.1128/9781555815547/e0164-01.gif
Untitled
Citation:
Ferry J.
2008.
Acetate-Based Methane Production,
p 155-170.
In
Wall J, Harwood C, Demain A (ed),
Bioenergy.
ASM Press, Washington, DC.
doi: 10.1128/9781555815547.ch13
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