Abstract
Carbon monoxide dehydrogenases (CODH) play an important role in utilizing carbon monoxide (CO) or carbon dioxide (CO2) in the metabolism of some microorganisms. Two distinctly different types of CODH are distinguished by the elements constituting the active site. A Mo-Cu containing CODH is found in some aerobic organisms, whereas a Ni-Fe containing CODH (henceforth simply Ni-CODH) is found in some anaerobes. Two members of the simplest class (IV) of Ni-CODH behave as efficient, reversible electrocatalysts of CO2/CO interconversion when adsorbed on a graphite electrode. Their intense electroactivity sets an important benchmark for the standard of performance at which synthetic molecular and material electrocatalysts comprised of suitably attired abundant first-row transition elements must be able to operate. Investigations of CODHs by protein film electrochemistry (PFE) reveal how the enzymes respond to the variable electrode potential that can drive CO2/CO interconversion in each direction, and identify the potential thresholds at which different small molecules, both substrates and inhibitors, enter or leave the catalytic cycle. Experiments carried out on a much larger (Class III) enzyme CODH/ACS, in which CODH is complexed tightly with acetyl-CoA synthase, show that some of these characteristics are retained, albeit with much slower rates of interfacial electron transfer, attributable to the difficulty in making good electronic contact at the electrode. The PFE results complement and clarify investigations made using spectroscopic investigations.
Keywords
Please cite as: Met. Ions Life Sci. 14 (2014) 71–97
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
S. W. Ragsdale, E. Pierce, Biochim. Biophys. Acta 2008, 1784, 1873–1898.
J. G. Ferry, Annu. Rev. Microbiol. 2010, 64, 453–473.
E. Oelgeschlaeger, M. Rother, Arch. Microbiol. 2008, 190, 257–269.
M. Can, F. A. Armstrong, S. W. Ragsdale, Chem. Rev. 2014, 114, 4119–4174.
O. Meyer, H. G. Schlegel, Annu. Rev. Microbiol. 1983, 37, 277–310.
G. Bender, E. Pierce, J. A. Hill, J. E. Darty, S. W. Ragsdale, Metallomics 2011, 3, 797–815.
H. Dobbek, L. Gremer, R. Kiefersauer, R. Huber, O. Meyer, Proc. Natl. Acad. Sci. USA 2002, 99, 15971–15976.
J. H. Jeoung, H. Dobbek, Science 2007, 318, 1461–1464.
D. A. Grahame, J. Biol. Chem. 1991, 266, 22227–22233.
P. A. Lindahl, B. Chang, Orig. Life Evol. Biosph. 2001, 31, 403–434.
S. W. Ragsdale, Crit. Rev. Biochem. Mol. Biol. 2004, 39, 165–195.
B. Soboh, D. Linder, R. Hedderich, Eur. J. Biochem. 2002, 269, 5712–5721.
J. D. Fox, Y. P. He, D. Shelver, G. P. Roberts, P. W. Ludden, J. Bacteriol. 1996, 178, 6200–6208.
J. H. Jeoung, H. Dobbek, J. Am. Chem. Soc. 2009, 131, 9922–9923.
H. Dobbek, V. Svetlitchnyi, J. Liss, O. Meyer, J. Am. Chem. Soc. 2004, 126, 5382–5387.
V. Svetlitchnyi, H. Dobbek, W. Meyer-Klaucke, T. Meins, B. Thiele, P. Romer, R. Huber, O. Meyer, Proc. Natl. Acad. Sci. USA. 2004, 101, 446–451.
A. Parkin, J. Seravalli, K. A. Vincent, S. W. Ragsdale, F. A. Armstrong, J. Am. Chem. Soc. 2007, 129, 10328–10329.
V. C. C. Wang, M. Can, E. Pierce, S. W. Ragsdale, F. A. Armstrong, J. Am. Chem. Soc. 2013, 135, 2198–2206.
V. C. C. Wang, S. W. Ragsdale, F. A. Armstrong, ChemBioChem 2013, 14, 1845–1851.
Y. Kung, T. I. Doukov, J. Seravalli, S. W. Ragsdale, C. L. Drennan, Biochemistry 2009, 48, 7432–7440.
C. L. Drennan, J. Y. Heo, M. D. Sintchak, E. Schreiter, P. W. Ludden, Proc. Natl. Acad. Sci. USA 2001, 98, 11973–11978.
C. Darnault, A. Volbeda, E. J. Kim, P. Legrand, X. Vernede, P. A. Lindahl, J. C. Fontecilla-Camps, Nat. Struct. Biol. 2003, 10, 271–279.
P. A. Lindahl, Angew. Chem. Int. Ed. 2008, 47, 4054–4056.
P. A. Lindahl, Biochemistry 2002, 41, 2097–2105.
P. Amara, J. M. Mouesca, A. Volbeda, J. C. Fontecilla-Camps, Inorg. Chem. 2011, 50, 1868–1878.
W. W. Gu, J. Seravalli, S. W. Ragsdale, S. P. Cramer, Biochemistry 2004, 43, 9029–9035.
G. O. Tan, S. A. Ensign, S. Ciurli, M. J. Scott, B. Hedman, R. H. Holm, P. W. Ludden, Z. R. Korsun, P. J. Stephens, K. O. Hodgson, Proc. Natl. Acad. Sci. USA 1992, 89, 4427–4431.
C. Y. Ralston, H. X. Wang, S. W. Ragsdale, M. Kumar, N. J. Spangler, P. W. Ludden, W. Gu, R. M. Jones, D. S. Patil, S. P. Cramer, J. Am. Chem. Soc. 2000, 122, 10553–10560.
P. A. Lindahl, E. Munck, S. W. Ragsdale, J. Biol. Chem. 1990, 265, 3873–3879.
N. J. Spangler, P. A. Lindahl, V. Bandarian, P. W. Ludden, J. Biol. Chem. 1996, 271, 7973–7977.
J. L. Craft, P. W. Ludden, T. C. Brunold, Biochemistry 2002, 41, 1681–1688.
J. Seravalli, M. Kumar, W. P. Lu, S. W. Ragsdale, Biochemistry 1995, 34, 7879–7888.
S. W. Ha, M. Korbas, M. Klepsch, W. Meyer-Klaucke, O. Meyer, V. Svetlitchnyi, J. Biol. Chem. 2007, 282, 10639–10646.
S. A. Ensign, M. R. Hyman, P. W. Ludden, Biochemistry 1989, 28, 4973–4979.
W. Gong, B. Hao, Z. Wei, D. J. Ferguson, T. Tallant, J. A. Krzycki, M. K. Chan, Proc. Natl. Acad. Sci. USA 2008, 105, 9558–9563.
J.-H. Jeoung, H. Dobbek, J. Biol. Inorg. Chem. 2012, 17, 167–173.
M. E. Anderson, P. A. Lindahl, Biochemistry 1994, 33, 8702–8711.
M. E. Anderson, V. J. Derose, B. M. Hoffman, P. A. Lindahl, J. Am. Chem. Soc. 1993, 115, 12204–12205.
V. J. DeRose, J. Telser, M. E. Anderson, P. A. Lindahl, B. M. Hoffman, J. Am. Chem. Soc. 1998, 120, 8767–8776.
H. Dobbek, V. Svetlitchnyi, L. Gremer, R. Huber, O. Meyer, Science 2001, 293, 1281–1285.
J. Feng, P. A. Lindahl, J. Am. Chem. Soc. 2004, 126, 9094–9100.
K. A. Vincent, A. Parkin, F. A. Armstrong, Chem. Rev. 2007, 107, 4366–4413.
C. Léger, P. Bertrand, Chem. Rev. 2008, 108, 2379–2438.
K. A. Vincent, F. A. Armstrong, Inorg. Chem. 2005, 44, 798–809.
C. Léger, S. J. Elliott, K. R. Hoke, L. J. C. Jeuken, A. K. Jones, F. A. Armstrong, Biochemistry 2003, 42, 8653–8662.
F. A. Armstrong, J. Hirst, Proc. Natl. Acad. Sci. USA 2011, 108, 14049–14054.
S. V. Hexter, T. Esterle, F. A. Armstrong, Phys. Chem. Chem. Phys. 2014, 16, 11822–11833.
V. Svetlitchnyi, C. Peschel, G. Acker, O. Meyer, J. Bacteriol. 2001, 183, 5134–5144.
S. W. Ragsdale, J. E. Clark, L. G. Ljungdahl, L. L. Lundie, H. L. Drake, J. Biol. Chem. 1983, 258, 2364–2369.
W. S. Shin, P. A. Lindahl, Biochim. Biophys. Acta 1993, 1161, 317–322.
J. Y. Heo, C. R. Staples, C. M. Halbleib, P. W. Ludden, Biochemistry 2000, 39, 7956–7963.
M. J. Lukey, A. Parkin, M. M. Roessler, B. J. Murphy, J. Harmer, T. Palmer, F. Sargent, F. A. Armstrong, J. Biol. Chem. 2010, 285, 20421–20421.
J. Q. Xia, J. F. Sinclair, T. O. Baldwin, P. A. Lindahl, Biochemistry 1996, 35, 1965–1971.
W. Shin, P. A. Lindahl, J. Am. Chem. Soc. 1992, 114, 9718–9719.
S. W. Ragsdale, H. G. Wood, J. Biol. Chem. 1985, 260, 3970–3977.
M. Kumar, W. P. Lu, S. W. Ragsdale, Biochemistry 1994, 33, 9769–9777.
E. L. Maynard, P. A. Lindahl, J. Am. Chem. Soc. 1999, 121, 9221–9222.
J. Seravalli, S. W. Ragsdale, Biochemistry 2000, 39, 1274–1277.
O. Lazarus, T. W. Woolerton, A. Parkin, M. J. Lukey, E. Reisner, J. Seravalli, E. Pierce, S. W. Ragsdale, F. Sargent, F. A. Armstrong, J. Am. Chem. Soc. 2009, 131, 14154–14155.
O. O. James, A. M. Mesubi, T. C. Ako, S. Maity, Fuel Process. Technol. 2010, 91, 136–144.
T. W. Woolerton, S. Sheard, E. Pierce, S. W. Ragsdale, F. A. Armstrong, Energy Environ. Sci. 2011, 4, 2393–2399.
Y. S. Chaudhary, T. W. Woolerton, C. S. Allen, J. H. Warner, E. Pierce, S. W. Ragsdale, F. A. Armstrong, Chem. Commun. 2012, 48, 58–60.
A. Bachmeier, V. C. C. Wang, T. W. Woolerton, S. Bell, J. C. Fontecilla-Camps, M. Can, S. W. Ragsdale, Y. S. Chaudhary, F. A. Armstrong, J. Am. Chem. Soc. 2013, 135, 15026–15032.
Acknowledgments
The authors thank the UK Research Councils (BBSRC (grants H003878-1 and BB/I022309) and EPSRC (Supergen 5, EH/H019480/1)), and NIH (GM39451) for supporting their research. Vincent Wang thanks the Ministry of Education, Taiwan (R.O.C) for financial support through a scholarship for study abroad.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Abbreviations
Abbreviations
- acetyl-CoA:
-
acetyl-coenzyme A
- ACDS:
-
acetyl-CoA decarbonylase synthase
- Ch :
-
Carboxydothermus hydrogenoformans
- CoA:
-
coenzyme A
- CODH:
-
carbon monoxide dehydrogenase
- CODH/ACS:
-
carbon monoxide dehydrogenase/acetyl-CoA synthase
- CoFeSP:
-
corrinoid-iron-sulfur protein
- E FB :
-
flatband potential
- EPR:
-
electron paramagnetic resonance
- Mb :
-
Methanosarcina barkeri
- MES:
-
2-(N-morpholino)ethanesulfonic acid
- Mt :
-
Moorella thermoacetica
- PDB:
-
Protein Data Base
- PFE:
-
protein film electrochemistry
- PGE:
-
pyrolytic graphite edge
- Rr :
-
Rhodospirillum rubrum
- SHE:
-
standard hydrogen electrode
- XAS:
-
X-ray absorption spectroscopy
Rights and permissions
Copyright information
© 2014 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Wang, V.CC., Ragsdale, S.W., Armstrong, F.A. (2014). Investigations of the Efficient Electrocatalytic Interconversions of Carbon Dioxide and Carbon Monoxide by Nickel-Containing Carbon Monoxide Dehydrogenases. In: Kroneck, P., Torres, M. (eds) The Metal-Driven Biogeochemistry of Gaseous Compounds in the Environment. Metal Ions in Life Sciences, vol 14. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-9269-1_4
Download citation
DOI: https://doi.org/10.1007/978-94-017-9269-1_4
Published:
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-017-9268-4
Online ISBN: 978-94-017-9269-1
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)