Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 433

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open α subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase

Darnault, Claudine, Volbeda, Anne, Kim, Eun Jin, Legrand, Pierre, Vernède, Xavier, Lindahl, Paul A., Fontecilla-Camps, Juan C.·2003·Nature Structural & Molecular Biology
DOI 10.1038/nsb912
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/nsb912

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 2 references

Research works printed but not linked: 48

  1. Wood, H.G. & Ljungdahl, L.G Autotrophic character of acetogenic bacteria. in Variation in Autotrophic Life (eds. Shively, J.M. & Barton, L.L.) 201–250 (Academic Press, New York; 1991).
  2. Dobbek, H., Svetlitchnyi, V., Gremer, L., Huber, R. & Meyer, O. Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster. Science 293, 1281–1285 (2001). · DOI · Paper page
  3. Drennan, C.L., Heo, J., Sintchak, M.D., Schreiter, E. & Ludden, P.W. Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proc. Natl. Acad. Sci. USA 98, 11973–11978 (2001). · DOI · Paper page
  4. Lindahl, P.A., Munck, E. & Ragsdale, S.W. CO dehydrogenase from Clostridium thermoaceticum. EPR and electrochemical studies in CO2 and argon atmospheres. J. Biol. Chem. 265, 3873–3879 (1990). · DOI
  5. Maynard, E.L. & Lindahl, P.A. Evidence of a molecular tunnel connecting the active sites for CO2 reduction and acetyl-CoA synthesis in acetyl-CoA synthase from Clostridium thermoaceticum. J. Am. Chem. Soc. 121, 9221–9222 (1999). · DOI
  6. Seravalli, J. & Ragsdale, S.W. Channeling of carbon monoxide during anaerobic carbon dioxide fixation. Biochemistry 39, 1274–1277 (2000). · DOI
  7. Doukov, T.I., Iverson, T.M., Seravalli, J., Ragsdale, S.W. & Drennan, C.L. A Ni-Fe-Cu center in a bifuctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science 298, 567–572 (2002). · DOI · Paper page
  8. Lu, W.P., Harder, S.R. & Ragsdale, S.W. Controlled potential enzymology of methyl transfer reactions involved in acetyl-CoA synthesis by CO dehydrogenase and the corrinoid/iron-sulfur protein from Clostridium thermoaceticum. J. Biol. Chem. 265, 3124–3133 (1990). · DOI
  9. Barondeau, D.P. & Lindahl, P.A. Methylation of carbon monoxide dehydrogenase from Clostridium thermoaceticum and the mechanism of acetyl-CoA synthesis. J. Am. Chem. Soc. 119, 3959–3970 (1997). · DOI
  10. Ragsdale, S.W. & Wood, H.G. Acetate biosynthesis by acetogenic bacteria. Evidence that carbon monoxide dehydrogenase is the condensing enzyme that catalyzes the final steps of the synthesis. J. Biol. Chem. 260, 3970–3977 (1985). · DOI · Paper page
  11. Tucci, G.C. & Holm, R.H. Nickel-mediated formation of thio esters from bound methyl, thiols, and carbon monoxide: a possible reaction pathway of acetyl-coenzyme A synthase activity in nickel-containing carbon monoxide dehydrogenases. J. Am. Chem. Soc. 117, 6489–6496 (1995). · DOI
  12. Montet, Y. et al. Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics. Nat. Struct. Biol. 4, 523–526 (1997). · DOI · Paper page
  13. Shin, W. & Lindahl, P.A. Function and CO binding properties of the NiFe complex in carbon monoxide dehydrogenase from Clostridium thermoaceticum. Biochemistry 31, 12870–12875 (1992). · DOI
  14. Tan, X.S., Sewell, C., Yang, Q. & Lindahl, P.A. Reduction and methyl transfer kinetics of the α subunit from acetyl-coenzyme A synthase. J. Am. Chem. Soc. 125, 318–319 (2003). · doi:10.1021/ja028442t
  15. Tan, X.S., Sewell, C. & Lindahl, P.A. Stopped-flow kinetics of methyl group transfer between the corrinoid-iron-sulfur protein and acetyl-coenzyme A synthase from Clostridium thermoaceticum. J. Am. Chem. Soc. 124, 6277–6284 (2002). · DOI
  16. Ragsdale, S.W., Ljungdahl, L.G. & Dervartanian, D.V. 13C and 61Ni isotope substitutions confirm the presence of a nickel(III)-carbon species in acetogenic CO dehydrogenases. Biochem. Biophys. Res. Commun 115, 658–665 (1983). · DOI
  17. Ragsdale, S.W., Wood, H.G. & Antholine, W.E. Evidence that an iron-nickel-carbon complex is formed by reaction of carbon monoxide with the carbon monoxide dehydrogenase from Clostridium thermoaceticum. Proc. Natl. Acad. Sci. USA 82, 6811–6814 (1985). · DOI
  18. Xia, J. & Lindahl, P.A. Assembly of an exchange-coupled [Ni:′Fe4S4] cluster in the α metallosubunit of CO dehydrogenase from Clostridium thermoaceticum with spectroscopic properties and CO-binding ability mimicking those of the acetyl-CoA synthase active site. J. Am. Chem. Soc. 118, 483–484 (1996). · DOI
  19. Russell, W.K., Stålhandske, C.M.V., Xia, J., Scott, R.A. & Lindahl, P.A. Spectroscopic, redox and structural characterization of the Ni-labile and nonlabile forms of the acetyl-CoA synthase active site of CO dehydrogenase. J. Am. Chem. Soc. 120, 7502–7510 (1998). · DOI
  20. Shin, W., Anderson, M.E. & Lindahl, P.A. Heterogeneous nickel environments in carbon monoxide dehydrogenase from Clostridium thermoaceticum. J. Am. Chem. Soc. 115, 5522–5526 (1993). · DOI
  21. Shin, W. & Lindahl, P.A. Low spin quantitation of NiFeC EPR signal from carbon monoxide dehydrogenase is not due to damage incurred during protein purification. Biochim. Biophys. Acta 1161, 317–322 (1993). · DOI
  22. Lindahl, P.A., Ragsdale, S.W. & Münck, E. Mössbauer study of CO dehydrogenase from Clostridium thermoaceticum. J. Biol. Chem. 265, 3880–3888 (1990). · DOI
  23. Wilson, B.E. & Lindahl, P.A. Equilibrium dialysis study and mechanistic implications of coenzyme A binding to acetyl-CoA synthase/carbon monoxide dehydrogenase from Clostridium thermoaceticum. J. Biol. Inorg. Chem. 4, 742–748 (1999). · doi:10.1007/s007750050346
  24. Musie, G., Farmer, P.J., Tuntulani, T., Reibenspies, J.H. & Darensbourg, M.Y. Influence of sulfur metalation on the accessibility of the NiII/I couple in [N, N′-Bis(2-mercaptoethyl)-1,5-diazacyclootanato]nickel(II): insight into the redox properties of [NiFe]-hydrogenase. Inorg. Chem. 35, 2176–2183 (1996). · doi:10.1021/ic9515968
  25. Lai, C.-H., Reibenspies, J.H. & Darensbourg, M.Y. Thiolate bridged nickel-iron complexes containing both iron(0) and iron(II) carbonyls. Angew. Chem. Int. Ed. Engl. 35, 2390–2393 (1996). · doi:10.1002/anie.199623901
  26. Bouwman, E., Henderson, R.K., Spek, A.L. & Reedijk, J. Spontaneous assembly of a novel tetranuclear Ni-Fe complex by complete reshuffling of ligands and oxidation states. Eur. J. Inorg. Chem. 1999, 217–219 (1999). · doi:10.1002/(sici)1099-0682(19990202)1999:2<217::aid-ejic217>3.0.co;2-n
  27. Tolman, C.A. Electron donor-acceptor properties of phosphorus ligands. Substituent additivity. J. Am. Chem. Soc. 92, 2953–2956 (1970). · doi:10.1021/ja00713a006
  28. Shultz, C.S., DeSimone, J.M. & Brookhart, M. Four- and five-coordinate CO insertion mechanisms in d8-nickel(II) complexes. J. Am. Chem. Soc. 123, 9172–9173 (2001). · doi:10.1021/ja0160896
  29. Tolman, C.A., Seidel, W.C. & Gosser, L.W. Formation of three-coordinate nickel(0) complexes by phosphorus ligand dissociation from NiL4 . J. Am. Chem. Soc. 96, 53–60 (1973). · doi:10.1021/ja00808a009
  30. Hsiao, Y.-M., Chojnacki, S.S., Hinton, P., Reibenspies, J.H. & Darensbourg, M.Y. Organometallic chemistry of sulfur/phosphorus donor ligand complexes of nickel(II) and nickel(0). Organometallics 12, 870–875 (1993). · DOI
  31. Volbeda, A. et al. Structure of the (NiFe) hydrogenase active site: evidence for biologically uncommon Fe ligands. J. Am. Chem. Soc. 118, 12989–12996 (1996). · DOI · Paper page
  32. Fan, C., Gorst, C.M., Ragsdale, S.W. & Hoffman, B.M. Characterization of the nickel-iron-carbon complex formed by reaction of carbon monoxide with the carbon monoxide dehydrogenase from Clostridium thermoaceticum by Q-band ENDOR. Biochemistry 30, 431–435 (1991). · DOI
  33. Collman, J.P., Hegedus, L.S., Norton, J.R. & Finke, R.G. Intramolecular insertion reactions. in Principles and Applications of Organotransition Metal Chemistry 355–399 (University Science Books, Mill Valley; 1987).
  34. Gencic, S. & Grahame, D.A. Nickel in subunit β of the acetyl-CoA decarbonylase/synthetase multienzyme complex in methanogens. J. Biol. Chem. 278, 6101–6110 (2003). · DOI
  35. Lundie, L.L. Jr. & Drake, H.L. Development of a minimally defined medium for the acetogen Clostridium thermoaceticum. J. Bacteriol. 159, 700–703 (1984). · DOI
  36. Vernède, X. & Fontecilla-Camps, J.C. A method to stabilize reduced and/or gas-treated protein crystals by flash-cooling under a controlled atmosphere. J. Appl. Crystallogr. 32, 505–509 (1999). · doi:10.1107/s0021889899002678
  37. Kabsch, W. Integration, scaling, space-group assignment and post refinement. in International Tables for Crystallography, Volume F, Crystallography of Biological Macromolecules (eds. Rossmann, M.G. & Arnold, E.) Ch. 11.3 (Kluwer Academic Publishers, Dordrecht; 2001).
  38. Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157–163 (1994). · DOI · Paper page
  39. Terwilliger, T.C. & Berendzen, J. Automated structure solution for MIR and MAD. Acta Crystallogr. D 55, 849–861 (1999). · DOI · Paper page
  40. Read, R.J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140–149 (1986). · DOI · Paper page
  41. Terwilliger, T.C. Map-likelihood phasing. Acta Crystallogr. D 57 1763–1775 (2001). · doi:10.1107/s0907444901013749
  42. Perrakis, A., Morris, R.J. & Lamzin, V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6, 458–463 (1999). · DOI
  43. Murshudov, G.N., Vagin, A.A. & Dodson, E.J. Refinement of macromolecular structures by the maximum-likehood method. Acta Crystallogr. D 53, 240–255 (1997). · DOI · Paper page
  44. Winn, M.D., Isupov, M.N. & Murshudov, G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D 57, 122–133 (2001). · DOI · Paper page
  45. Volbeda, A. Spéléologie des hydrogenases à nickel et à fer. Les écoles physique et chimie du vivant 1, 47–52 (1999).
  46. Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946–950 (1991). · DOI · Paper page
  47. Merritt, E.A. & Bacon, D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505–524 (1997). · DOI · Paper page
  48. Lawrence, M.C. & Bourke, P. A program for generating electron density isosurfaces from Fourier syntheses in protein crystallography. J. Appl. Crystallogr. 33, 990–991 (2000). · DOI

Cited by

See all 433

Metadata

Authors
Darnault, C., Volbeda, A., Kim, E. J., Legrand, P., Vernède, X., Lindahl, P. A., & Fontecilla-Camps, J. C.
Venue
Nature Structural & Molecular Biology
Publisher
Springer Science and Business Media LLC
Published
2003-03-10
Volume
10
Issue
4
Pages
271-279
ISSN
  • 1545-9985 (ISSN-L)
  • 1545-9993
DOI
10.1038/nsb912
OpenAlex
W2019528254
Cited by
433
References
2
FWCI
27.84
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open α subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase. https://app.cochat.ai/papers/10.1038/nsb912
The paper
Darnault, C., Volbeda, A., Kim, E. J., Legrand, P., Vernède, X., Lindahl, P. A., & Fontecilla-Camps, J. C. (2003). Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open α subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsb912

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.