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Enzymology of the Wood–Ljungdahl Pathway of Acetogenesis

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Ragsdale, Stephen W.·2008·Annals of the New York Academy of Sciences
DOI 10.1196/annals.1419.015
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Abstract

The biochemistry of acetogenesis is reviewed. The microbes that catalyze the reactions that are central to acetogenesis are described and the focus is on the enzymology of the process. These microbes play a key role in the global carbon cycle, producing over 10 trillion kilograms of acetic acid annually. Acetogens have the ability to anaerobically convert carbon dioxide and CO into acetyl‐CoA by the Wood–Ljungdahl pathway, which is linked to energy conservation. They also can convert the six carbons of glucose stoichiometrically into 3 mol of acetate using this pathway. Acetogens and other anaerobic microbes (e.g., sulfate reducers and methanogens) use the Wood–Ljungdahl pathway for cell carbon synthesis. Important enzymes in this pathway that are covered in this review are pyruvate ferredoxin oxidoreductase, CO dehydrogenase/acetyl‐CoA synthase, a corrinoid iron‐sulfur protein, a methyltransferase, and the enzymes involved in the conversion of carbon dioxide to methyl‐tetrahydrofolate.

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Research works printed but not linked: 85

  1. Ragsdale S.W., 2006, Biological Inorganic Chemistry: Structure and Reactivity, 452
  2. 10.1080/10409230490496577 · DOI · Paper page
  3. Drake H.L.2008.Old acetogens new light. Ann. N.Y. Acad Sci. Incredible Anaerobes: From Physiology to Genomics to Fuels. In Press. · DOI · Paper page
  4. 10.1128/JB.43.6.701-715.1942 · DOI · Paper page
  5. 10.3109/10409239209082570 · DOI · Paper page
  6. 10.1128/JB.187.7.2386-2394.2005 · doi:10.1128/jb.187.7.2386-2394.2005
  7. 10.1074/jbc.M412118200 · DOI
  8. 10.1016/j.str.2004.03.007 · DOI
  9. Ragsdale S.W., 1997, The Eastern and Western branches of the Wood/Ljungdahl pathway: how the East and West were won, BioFactors, 9, 1
  10. 10.1007/978-1-4615-1777-1_1 · DOI · Paper page
  11. Lajoie S.F., 1988, Acetate production from hydrogen and [13C]carbon dioxide by the microflora of human feces, Appl. Environ. Microbiol., 54, 2723, 10.1128/aem.54.11.2723-2727.1988 · DOI
  12. 10.1128/AEM.52.4.623-630.1986 · DOI · Paper page
  13. 10.1111/j.1574-6968.1990.tb04929.x · DOI
  14. 10.1111/j.1432-1033.1996.0035n.x · DOI
  15. 10.1007/978-1-4615-2391-8_11 · DOI
  16. 10.1074/jbc.274.42.29772 · DOI
  17. 10.1093/oxfordjournals.molbev.a026218 · DOI
  18. 10.1038/5870 · DOI
  19. 10.1016/0969-2126(93)90025-C · DOI · Paper page
  20. 10.1021/bi0257641 · DOI
  21. 10.1021/ja01564a064 · DOI · Paper page
  22. Drake H.L., 1981, Purification of five components from Clostridium thermoacticum which catalyze synthesis of acetate from pyruvate and methyltetrahydrofolate. Properties of phosphotransacetylase, J. Biol. Chem., 256, 11137, 10.1016/S0021-9258(19)68568-6 · DOI · Paper page
  23. 10.1021/bi961014d · DOI
  24. Schulman M., 1973, Total synthesis of acetate from CO2. VII. Evidence with Clostridium thermoaceticum that the carboxyl of acetate is derived from the carboxyl of pyruvate by transcarboxylation and not by fixation of CO2, J. Biol. Chem., 248, 6255
  25. 10.1126/science.1066198 · DOI · Paper page
  26. 10.1021/bi0602516 · DOI
  27. 10.1021/ja0585275 · DOI
  28. 10.1021/bi970403k · DOI
  29. 10.1046/j.1432-1327.1999.00648.x · DOI
  30. 10.1016/j.jinorgbio.2007.07.014 · DOI
  31. 10.1128/JB.183.17.5134-5144.2001 · DOI · Paper page
  32. 10.1515/BC.2000.108 · DOI
  33. Meyer O., 1993, Microbial Growth on C1 Compounds, 433
  34. 10.1021/bi026514n · DOI
  35. 10.1074/jbc.275.9.6234 · DOI
  36. 10.1073/pnas.96.16.8884 · DOI · Paper page
  37. 10.1073/pnas.211429998 · DOI · Paper page
  38. 10.1126/science.1075843 · DOI · Paper page
  39. 10.1126/science.1061500 · DOI · Paper page
  40. 10.1038/nsb912 · DOI · Paper page
  41. 10.1021/ja037776v · doi:10.1021/ja037776v
  42. 10.1021/ic062362z · DOI
  43. 10.1021/bi036062u · DOI
  44. 10.1007/s00775-004-0563-y · DOI
  45. 10.1021/ja073643o · DOI · Paper page
  46. Fontecilla‐Camps J.‐C., 1999, Advances in Inorganic Chemistry, 283
  47. 10.1021/bi982473c · DOI
  48. 10.1016/0006-291X(82)90880-4 · DOI
  49. 10.1021/bi991812e · DOI
  50. 10.1021/ja992120g · DOI
  51. 10.1073/pnas.0304262101 · DOI · Paper page
  52. 10.1021/bi060003 · doi:10.1021/bi060003
  53. 10.1007/s00775-004-0564-x · DOI
  54. 10.1007/s00775-004-0566-8 · DOI
  55. 10.1021/bi011687i · DOI
  56. 10.1021/ja00066a021 · DOI
  57. 10.1021/ja963597k · DOI
  58. 10.1021/bi036194n · DOI
  59. Lu W.P., 1991, Reductive activation of the coenzyme A/acetyl‐CoA isotopic exchange reaction catalyzed by carbon monoxide dehydrogenase from Clostridium thermoaceticum and its inhibition by nitrous oxide and carbon monoxide, J. Biol. Chem., 266, 3554, 10.1016/S0021-9258(19)67831-2 · DOI
  60. 10.3109/10409239109114070 · DOI · Paper page
  61. 10.1016/S0076-6879(78)53042-5 · DOI
  62. 10.1007/BF00411642 · DOI
  63. 10.1021/bi00476a007 · DOI
  64. Moore M.R., 1974, Purification and characterization of nicotinamide adenine dinucleotide‐dependent methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum, J. Biol. Chem., 249, 5250, 10.1016/S0021-9258(19)42355-7 · DOI
  65. 10.1016/S0021-9258(18)90590-9 · DOI
  66. Park E.Y., 1991, Chemistry and Biochemistry of Flavoenzymes, 389
  67. Hu S.‐I., 1984, Acetate synthesis from carbon monoxide by Clostridium thermoaceticum. Purification of the corrinoid protein, J. Biol. Chem., 259, 8892, 10.1016/S0021-9258(17)47238-3 · DOI
  68. Ragsdale S.W., 1987, Mössbauer, EPR, and optical studies of the corrinoid/Fe‐S protein involved in the synthesis of acetyl‐CoA by Clostridium thermoaceticum, J. Biol. Chem., 262, 14289, 10.1016/S0021-9258(18)47936-7 · DOI · Paper page
  69. 10.1146/annurev.biochem.72.121801.161828 · DOI · Paper page
  70. 10.1128/jb.176.19.6127-6130.1994 · DOI
  71. Lu W.‐P., 1993, Sequence and expression of the gene encoding the corrinoid/iron‐sulfur protein from Clostridium thermoaceticum and reconstitution of the recombinant protein to full activity, J. Biol. Chem., 268, 5605, 10.1016/S0021-9258(18)53364-0 · DOI
  72. Doukov T., 1995, Preliminary X‐ray diffraction analysis of the methyltetrahydrofolate:corrinoid/iron sulfur protein methyltransferase from Clostridium themoaceticum, Acta Crystallographa., 51, 1092
  73. 10.1074/jbc.M609828200 · DOI
  74. 10.1021/bi9824745 · DOI
  75. 10.1016/S0969-2126(00)00172-6 · DOI
  76. 10.1073/pnas.0601420103 · DOI · Paper page
  77. 10.1021/bi001431x · DOI
  78. 10.1021/bi00046a013 · DOI
  79. 10.1021/ar0000051 · DOI · Paper page
  80. 10.1074/jbc.274.17.11513 · DOI
  81. 10.1021/bi9727996 · DOI
  82. 10.1073/pnas.0308082100 · DOI
  83. 10.1021/bi060051u · doi:10.1021/bi060051u
  84. 10.1126/science.282.5395.1853 · DOI · Paper page
  85. 10.1016/S0968-0004(99)01536-4 · DOI · Paper page

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Metadata

Authors
Ragsdale, S. W.
Venue
Annals of the New York Academy of Sciences
Publisher
Wiley
Published
2008-03
Volume
1125
Issue
1
Pages
129-136
ISSN
  • 0077-8923 (ISSN-L)
  • 1749-6632
DOI
10.1196/annals.1419.015
OpenAlex
W2114450960
Cited by
383
References
3
FWCI
3.47
Type
journal article
Language
en
Open access
green
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 25 d)

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CoChat. (2026). Citation check: Enzymology of the Wood–Ljungdahl Pathway of Acetogenesis. https://app.cochat.ai/papers/10.1196/annals.1419.015
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Ragsdale, S. W. (2008). Enzymology of the Wood–Ljungdahl Pathway of Acetogenesis. Annals of the New York Academy of Sciences. https://doi.org/10.1196/annals.1419.015

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