Abstract
This chapter deals with the enzymatic conversion of CO2. It covers the two aspects of the fixation of the entire CO2 molecule into substrates (carboxylation) and the reduction of CO2 to other C1 (or C2) energy-richer molecules. The known mechanisms are discussed and barriers to exploitation at the industrial level highlighted.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsReferences
Tong X, El-Zahab B, Zhao X, Liu Y, Wang P (2011) Enzymatic synthesis of L-lactic acid from carbon dioxide and ethanol with an inherent cofactor regeneration cycle. Biotechnol Bioeng 108(2):465–469
Park SW, Joo OS, Jung KD, Kim H, Han SH (2001) Development of ZnO/Al2O3 catalyst for reverse-water-gas-shift reaction of CAMERE (carbon dioxide hydrogenation to form methanol via a reverse-water-gas-shift reaction) process. Appl Catal A Gen 211:81–90
Azuma M, Hashimoto K, Hiromoto M (1990) Electrochemical reduction of carbon dioxide on various metal electrodes in low-temperature aqueous KHCO3 media. J Electrochem Soc 137:1772–1778
Subrahmanyam M, Kaneco S, Alonso-Vante N (1999) A screening for the photo reduction of carbon dioxide supported on metal oxide catalysts for C1–C3 selectivity. Appl Catal B Environ 23(2–3):169–174
Kuwabata S, Nishida K, Tsuda R, Inoue H, Yoneyama H (1994) Photochemical reduction of carbon dioxide to methanol using ZnS microcrystallite as a photocatalyst in the presence of methanol dehydrogenase. J Electrochem Soc 141(6):1498–1503
Aresta M, Quaranta E, Liberio R, Dileo C, Tommasi I (1998) Enzymatic synthesis of 4-OH-benzoic acid from phenol and CO2: the first example of a biotechnological application of a carboxylase enzyme. Tetrahedron 54(30):8841–8846
Dave BC, Obert R (1999) Enzymatic conversion of carbon dioxide to methanol: enhanced methanol production in silica sol-gel matrices. J Am Chem Soc 121:12192–12193
Field CB, Behrenfeld MJ, Randerson JT, Falkowski P (1998) Primary production of the biosphere: integrating terrestrial and oceanic components. Science 281:237–240
Thauer RK, Kaster A-K, Seedorf H, Buckel W, Hedderich R (2008) Methanogenic archaea: ecologically relevant differences in energy conservation. Nat Rev Microbiol 6:579–591
Hugler M, Huber H, Stetter KO, Fuchs G (2003) Autotrophic CO2 fixation pathways in archaea (Crenarchaeota). Arch Microbiol 179:160–173
Glueck SM, Gumus S, Fabian WMF, Faber K (2010) Biocatalytic carboxylation. Chem Soc Rev 39:313–328
Calvin M (1961) Nobel prize for chemistry: Prof. M. Calvin, For. Mem. R.S. Nature 192:799
Hartman FC, Harpel MR (1994) Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase/oxygenase. Annu Rev Biochem 63:197–234
Evans MC, Buchanan BB, Arnon DI (1966) A new ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium. Proc Natl Acad Sci USA 55:928–934
Ljungdahl LG (1986) The autotrophic pathway of acetate synthesis in acetogenic bacteria. Annu Rev Microbiol 40:415–450
Drake HL, Goßner AS, Daniel SL (2008) Old acetogens, new light. In: Wiegel, J (ed.) Incredible anaerobes. Ann N Y Acad Sci, 1125:100–128
Ragsdale SW, Pierce E (2008) Acetogenesis and Wood-Ljungdahl pathway of CO2 fixation. Biochim Biophys Acta 1784:1873–1898
Herter S, Fuchs G, Bacher A, Eisenreich W (2002) A bicyclic autotrophic CO2 fixation pathway in Chloroflexus aurantiacus. J Biol Chem 277:20277–20283
Alber B, Olinger M, Rieder A, Kockelkorn D, Jobst B, Hugler M, Fuchs G (2006) Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in Archaeal Metallosphaera and Sulfolobus spp. J Bacteriol 188:8551–8559
Berg IA, Kockelkorn D, Buckel W, Fuchs G (2007) A 3-hydroxypropionate/4-hydroxy-butyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318:1782–1786
Huber H, Gallenberger M, Jahn U, Eylert E, Berg IA, Kockelkorn D, Eisenreich W, Fuchs G (2008) A dicarboxylate/4-hydroxybutyrate autotrophic carbon assimilation cycle in the hyperthermophilic Archaeum Ignococcus hospitalis. Proc Natl Acad Sci USA 105:7851–7856
Erb TJ, Berg IA, Brecht V, Muller M, Fuchs G, Alber BE (2007) Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA carboxylase/reductase: the ethylmalonyl-CoA pathway. Proc Natl Acad Sci USA 104:10631–10636
Andersson I, Backlund A (2008) Structure and function of Rubisco. Plant Physiol Biochem 46:275–291
Bowyer JR, Leegood RC (1997) Photosynthesis. In: Dey P, Harborne J (eds) Plant biochemistry. Academic, New York, pp 49–110
Ellis RJ (1979) The most abundant protein in the world. Trends Biochem Sci 4:241–244
Schneider G, Lindqvist Y, Branden C-I (1992) RUBISCO: structure and mechanism. Annu Rev Biophys Biomol Struct 21:119–143
Phillips R, Milo R (2009) A feeling for the numbers in biology. Proc Natl Acad Sci USA 106:21465–21471
Buchanan BB, Arnon DI (1990) A reverse KREBS cycle in photosynthesis: consensus at last. Photosynth Res 24:47–53
Aoshima M (2007) Novel enzyme reactions related to the tricarboxylic acid cycle: phylogenetic/functional implications and biotechnological applications. Appl Microbiol Biotechnol 75:249–255
Berg IA (2011) Ecological aspects of the distribution of different autotrophic CO2 fixation pathways. Appl Environ Microbiol 77:1925–1936
Boyd JM, Ensign SA (2005) ATP-dependent enolization of acetone by acetone carboxylase from Rhodobacter capsulatus. Biochemistry 44:8543–8553
Mai XH, Adams MWW (1996) Characterization of a fourth type of 2-keto acid-oxidizing enzyme from a hyperthermophilic archaeon: 2-ketoglutarate ferredoxin oxidoreductase from Thermococcus litoralis. J Bacteriol 178:5890–5896
Ragsdale SW (2003) Pyruvate ferredoxin oxidoreductase and its radical intermediate. Chem Rev 103:2333–2346
Schut GJ, Menon AL, Adams MWW (2001) 2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol 331:144–158
Ragsdale SW (2007) Nickel and the carbon cycle. J Inorg Biochem 101:1657–1666
Ragsdale SW (2004) Life with carbon monoxide. Crit Rev Biochem Mol Biol 39:165–195
Lindahl PA, Chang B (2001) The evolution of acetyl-CoA synthase. Orig Life Evol Biosph 31:403–434
Hugler M, Krieger RS, Jahn M, Fuchs G (2003) Characterization of acetyl-CoA/propionyl-CoA carboxylase in Metallosphaera sedula. Eur J Biochem 270:736–744
Jahn U, Huber H, Eisenreich W, Hugler M, Fuchs G (2007) Insights into the autotrophic CO2 fixation pathway of the Archaeon Ignicoccus hospitalis: comprehensive analysis of the central carbon metabolism. J Bacteriol 189:4108–4119
Aresta M, Forti G (eds) (1987) Carbon dioxide as a source of carbon. Elsevier
Aresta M, Schloss JV (eds) (1990) Enzymatic and model reaction for carbon dioxide carboxylation and reduction reactions. Elsevier
Aresta M, Quaranta E, Tommasi I, Giannoccaro P, Ciccarese A (1995) Enzymatic versus chemical carbon dioxide utilisation. Part I. The role of metal centres in carboxylation reactions. Gazz Chim Ital 125:509–538
Kolbe H (1860) Ueber Synthese der Salicylsäure Justus Liebigs. Annalen der Chemie 113(1):125–127
Ota K (1974) Conversion reaction of alkali 4-hydroxyisophthalates to hydroxybenzoic acids. Bull Chem Soc Jpn 47:2343–2344
Fumasoni S, Pochetti F, Roberti G (1974) Simultaneous manufacture of urea and glycol, Ger Offen 2,318,327, CA, 80, 14593j
Fromm D, Luetzow D (1979) Modern methods of industrial chemistry: urea. Chem Unserer Zeit 13:78–81
Aresta M, Tommasi I, Dileo C, Dibenedetto A, Narracci M (2001) Biotechnological synthesis of 4-OH benzoate mediated by a phenylphosphate-carboxylase enzyme 221st National Meeting, American Chemical Society, San Diego, CA, April 1–5, Inorganic division, Abstract n° 581
Lack A, Fuchs G, Aresta M, Tommasi I (1991) Catalytic properties of phenol carboxylase of Pseudomonas aeruginosa (strain from Venice lagoon). Eur J Biochem 197:473
Platen H, Schink B (1987) Methanogenic degradation of acetone by an enrichment culture. Arch Microbiol 149:136–141
Schnell S, Bak F, Pfenng N (1989) Anaerobic degradation of aniline and dihydroxybenzenes by newly isolated sulfate-reducing bacteria and description of desulfobacterium aniline. Arch Microbiol 152:556–563
Aresta M, Dibenedetto A (2002) Development of environmentally friendly syntheses: use of enzymes and biomimetic systems for the direct carboxylation of organic substrates. Rev Mol Biotechnol 90:113–128
Dibenedetto A, Lo Noce R, Pastore C, Aresta M, Fragale C (2006) First in vitro use of the phenylphosphate carboxylase enzyme in supercritical CO2 for the selective carboxylation of phenol to 4-hydroxybenzoic acid. Environ Chem Lett 3:145–148
Ding B, Schmeling S, Fuchs G (2008) Anaerobic metabolism of catechol by the denitrifying bacterium Thauera aromatica – a result of promiscuous enzymes and regulators. J Bacteriol 190:1620–1630
Zhang X, Wiegel J (1994) Reversible conversion of 4-hydroxybenzoate and phenol by Clostridium hydroxybenzoicum. Appl Environ Microbiol 60:4182–4185
He Z, Wiegel J (1995) Purification and characterization of an oxygen-sensitive reversible 4-hydroxybenzoate decarboxylase from Clostridium hydroxybenzoicum. Eur J Biochem 229:77–82
He Z, Wiegel J (1996) Purification and characterization of an oxygen-sensitive reversible 3,4-dihydroxybenzoate decarboxylase from Clostridium hydroxybenzoicum. J Bacteriol 178:3539–4343
Miyazaki M, Shibue M, Ogino K, Nakamura H, Maeda H (2001) Enzymatic synthesis of pyruvic acid from acetaldehyde and carbon dioxide. Chem Commun 1800–1801
Wieser M, Yoshida T, Nagasawa T (2001) Carbon dioxide fixation by reversible pyrrole-2-carboxylate decarboxylase and its application. J Mol Catal B Enzym 11:179–184
Omura H, Wieser M, Nagasawa T (1998) Pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910, an organic-acid-requiring enzyme. Eur J Biochem 253:480–484
Wuensch C, Glueck SM, Gross J, Koszelewski D, Schober M, Faber K (2012) Regioselective enzymatic carboxylation of phenols and hydroxystyrene derivatives. Org Lett 14(8):1974–1977
Yoshida T, Fujita K, Nagasawa T (2002) Novel reversible indole-3-carboxylate decarboxylase catalyzing nonoxidative decarboxylation. Biosci Biotechnol Biochem 66(11):2388–2394
Rodriguez H, Landete JM, Curiel JA, de las Rivas B, Mancheno JM, Munoz R (2008) Characterization of the p-coumaric acid decarboxylase from Lactobacillus plantarum CECT 748(T). J Agric Food Chem 56:3068–3072
Cavin J-F, Barthelmebs L, Divies C (1997) Molecular characterization of an inducible p-coumaric acid decarboxylase from Lactobacillus plantarum: gene cloning, transcriptional analysis, overexpression in Escherichia coli, purification, and characterization. Appl Environ Microbiol 63:1939–1944
Gu W, Li X, Huang J, Duan Y, Meng Z, Zhang K-Q, Yang J (2011) Cloning, sequencing, and overexpression in Escherichia coli of the Enterobacter sp. Px6-4 gene for ferulic acid decarboxylase. Appl Microbiol Biotechnol 89:1797–1805
Prim N, Pastor FIJ, Diaz P (2003) Biochemical studies on cloned Bacillus sp. BP-7 phenolic acid decarboxylase PadA. Appl Microbiol Biotechnol 63:51–56
Goto M, Hayashi H, Miyahara I, Hirotsu K, Yoshida M, Oikawa T (2006) Crystal structures of nonoxidative Zn-dependent 2,6-dihydroxybenzoate (γ-resorcylate) decarboxylase from Rhizobium sp. strain Mtp-10005. J Biol Chem 281:34365–34373
Matte A, Grosse S, Bergeron H, Abokitse K, Lau PCK (2010) Structural analysis of Bacillus pumilus phenolic acid decarboxylase, a lipocalin-fold enzyme. Acta Crystallogr F66:1407–1414
Gu W, Yang J, Lou Z, Liang L, Sun Y, Huang J, Li X, Cao Y, Meng Z, Zhang K-Q (2011) Structural basis of enzymatic activity for the ferulic acid decarboxylase (FADase) from Enterobacter sp. p x6–4. PLoS One 6(1):e16262. doi:10.1371/journal.pone.0016262
Rodriguez H, Angulo I, de las Rivas B, Campillo N, Paez JA, Munoz R, Mancheno JM (2010) p-Coumaric acid decarboxylase from Lactobacillus plantarum: structural insights into the active site and decarboxylation catalytic mechanism. Proteins 78:1662–1676
Swaving J, de Bont JAM (1998) Microbial transformation of epoxides. Enzym Microb Technol 22(1):19–26
Allen JR, Ensign SA (1996) Carboxylation of epoxides to beta-keto acids in cell extracts of Xanthobacter strain Py2. J Bacteriol 178(5):1469–1472
Volbeda A, Fontecilla-Camps JC (2005) Structural bases for the catalytic mechanism of Ni-containing carbon monoxide dehydrogenases. Dalton Trans 3443–3450
Park SW, Taeksun S, Kim SY, Kim E, Oh J, Eom C, Kim YM (2007) Carbon monoxide dehydrogenase in mycobacteria possesses a nitric oxide dehydrogenase activity. Biochem Biophys Res Commun 362:449–453
Dobbek H, Gremer L, Meyer O, Huber R (1999) Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine. Proc Natl Acad Sci USA 96(16):8884–8889
Kato N, Sahm H, Wagner F (1979) Steady-state kinetics of formaldehyde dehydrogenase and formate dehydrogenase from a methanol-utilizing yeast, Candida boidinii. Biochim Biophys Acta Enzymol 566:12–20
Ljungdahl LG, Wood HG (1969) Total synthesis of acetate from CO2 by heterotrophic bacteria. Annu Rev Microbiol 23:515–538
Lu Y, Jiang ZY, Xu SW, Wu H (2006) Efficient conversion of CO2 to formic acid by formate dehydrogenase immobilized in a novel alginate-silica hybrid gel. Catal Today 115:263–268
Miyatani R, Amao Y (2002) Bio-CO2 fixation with formate dehydrogenase from Saccharomyces cerevisiae and water-soluble zinc porphyrin by visible light. Biotechnol Lett 24:1931–1934
Parkinson BA, Weaver PF (1984) Photoelectrochemical pumping of enzymatic CO2 reduction. Nature 309:148–149
Reda T, Plugge CM, Abram NJ, Hirst J (2008) Reversible interconversion of carbon dioxide and formate by an electroactive enzyme. Proc Natl Acad Sci USA 105:10654–10658
Ruschig U, Müller U, Willnow P, Höpner T (1976) CO2 reduction to formate by NADH catalyzed by formate dehydrogenase from Pseudomonas oxalaticus. Eur J Biochem 70:325–330
Boyington JC, Gladyshev VN, Khangulov SV, Stadtman TC, Sun PD (1997) Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. Science 275:1305–1308
Kraulis K (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946–950
Bacon DJ, Anderson WF (1988) A fast algorithm for rendering space-filling molecule pictures. J Mol Graph 6:219–220
Merritt EA, Murphy MEP (1994) Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr D50:869–873
Tsuru D (1979) Formaldehyde dehydrogenase from Pseudomonas putida. Purification and some properties. J Biochem 85(5):1165–1172
Tanaka N, Kusakabe Y, Ito K, Yoshimoto T, Nakamura KT (2002) Crystal structure of formaldehyde dehydrogenase from Pseudomonas putida: the structural origin of the tightly bound cofactor in nicotinoprotein dehydrogenases. J Mol Biol 324:519–533
Negelein E, Wulff HJ (1937) Diphosphopyridinproteid ackohol, acetaldehyd. Biochem Z 293:351–389
Theorell H, McKEE JS (1961) Mechanism of action of liver alcohol dehydrogenase. Nature 192(4797):47–50
Jörnvall H, Harris JI (1970) Horse liver alcohol dehydrogenase. On the primary structure of the ethanol-active isoenzyme. Eur J Biochem 13(3):565–576
Brändén CI, Eklund H, Nordström B, Boiwe T, Söderlund G, Zeppezauer E, Ohlsson I, Akeson A (1973) Structure of liver alcohol dehydrogenase at 2.9-Angstrom resolution. Proc Natl Acad Sci USA 70(8):2439–2442
Raaijmakers H, Macieira S, Dias JM, Teixeira S, Bursakov S, Huber R, Moura JJG, Moura I, Romão MJ (2002) Gene sequence and the 1.8 Å crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas. Structure 10:1261–1272
Kletzin A, Adams MWW (1996) Tungsten in biological systems. FEMS Microbiol Rev 18:5–63
de Bok FAM, Hagedoorn P-L, Silva PJ, Hagen WR, Schiltz E, Fritsche K, Stams AJM (2003) Two W-containing formate dehydrogenases (CO2-reductases)involved in syntrophic propionate oxidation by Syntrophobacter fumaroxidans. Eur J Biochem 270:2476–2485
Aresta M (2010) CO2 enzymatic carboxylation and reduction to methanol. International Scientific Forum on CO 2 chemistry and biochemistry, CO2 Challenge Forum, Lyon
Kima S, Kimb MK, Leeb SH, Yoonc S, Junga K-D (2014) Conversion of CO2- to formate in an electro-enzymatic cell using Candida boidinii formate dehydrogenase. J Mol Catal B Enzym 102:9–15
Jiang Z, Xu S, Wu H (2003) Novel conversion of carbon dioxide to methanol catalyzed by sol-gel immobilized dehydrogenases. International conference on carbon dioxide utilization ICCDU VII, Seoul-Korea
Xu S, Lu Y, Li J, Jiang Z, Wu H (2006) Efficient conversion of CO2 to methanol catalyzed by three dehydrogenases Co-encapsulated in an alginate-silica (ALG–SiO2) hybrid gel. Ind Eng Chem Res 45:4567–4573
Dibenedetto A, Stufano P, Baran T, Macyk W, Aresta M (2011) Hybrid technologies for an enhanced carbon recycling based on enzymatic CO2 reduction to methanol in water. International conference on carbon dioxide utilization ICCDU XI, Dijon, FR
Dibenedetto A, Angelini A, Aresta M, Macyk W, Baran T (2013) Nanomaterials as photocatalysts for the CO2 reduction to methanol in water. International conference on carbon dioxide utilization, ICCDU XII, Alexandria, VA
Dibenedetto A, Baran T, Macyk W, Aresta M (2013) Photonanomaterials for CO2 reduction to methanol. 245th ACS national meeting, New Orleans
Dibenedetto A, Stufano P, Angelini A, Fragale C, Aresta M, Costa M (2012) Hybrid technologies for an enhanced carbon recycling based on enzymatic CO2 reduction to methanol in water: chemical and photochemical NADH regeneration. ChemSusChem 5:373–378
Cazelles R, Drone J, Fajula F, Ersen O, Moldovan S, Galarneau A (2013) Reduction of CO2 to methanol by a polyenzymatic system encapsulated in phospholipids–silica nanocapsules. New J Chem 37:3721–3730
Song J, Kim Y, Lim M, Lee H, Lee JI, Shin W (2011) Microbes as electrochemical CO2 conversion catalysts. ChemSusChem 4:587–590
Aresta M, Dibenedetto A, Baran T, Angelini A, Łabuz P, Macyk W (2014) An integrated photocatalytic-enzymatic system for the reduction of CO2 to methanol in bio-glycerol-water. Beilstein J Org Chem 10:2556–2565
Aresta M, Dibenedetto A, Baran T, Macyk W (2013) Patent application MI2013A001135
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 2016 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Aresta, M., Dibenedetto, A., Quaranta, E. (2016). Enzymatic Conversion of CO2 (Carboxylation Reactions and Reduction to Energy-Rich C1 Molecules). In: Reaction Mechanisms in Carbon Dioxide Conversion. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-46831-9_9
Download citation
DOI: https://doi.org/10.1007/978-3-662-46831-9_9
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-662-46830-2
Online ISBN: 978-3-662-46831-9
eBook Packages: Chemistry and Materials ScienceChemistry and Material Science (R0)