The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
A Mixed-Valent, Fe(II)Fe(I), Diiron Complex Reproduces the Unique Rotated State of the [FeFe]Hydrogenase Active Site
Abstract
The fully reversible Fe I Fe I ⇆ Fe I Fe II couple of an N-heterocyclic carbene dinuclear Fe I Fe I complex, (μ-pdt)[Fe I (CO) 2 (PMe 3 )][Fe I (CO) 2 (IMes)], complex D, has led to the isolation of the mixed-valent cationic complex D ox as a biomimetic of the 2Fe2S subsite of the oxidized H cluster in [FeFe]hydrogenase. During the review of this submission a second complex was reported. As compared to complex D, a remarkable reorientation of the IMes NHC ligand enables the (μ-pdt)[Fe(CO) 2 (PMe 3 )][Fe(CO) 2 (IMes)] + cation, D ox, to exist as a “rotated” structure, with structural and spectroscopic similarities to the diiron unit of H as isolated or H ox . The structural makeup of the model includes an Fe−Fe distance that matches that of the enzyme, a semi-bridging CO group, and a pseudo-octahedral iron with open site blocked by a strategically positioned arene group from the IMes−NHC carbene ligand.
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.
Integrity signals
Registry
Cites
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.
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
Nicolet, Y., de Lacey, A. L., Vernède, X., Fernandez, V. M., Hatchikian, E. C., & Fontecilla-Camps, J. C. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0020963 · Cited by 786
Synthesis of the H-cluster framework of iron-only hydrogenase
Tard, C., Liu, X., Ibrahim, S. K., Bruschi, M., Gioia, L. D., Davies, S. C., Yang, X., Wang, L.-S., Sawers, G., & Pickett, C. J. (2005) · Nature · doi:10.1038/nature03298 · Cited by 508
A novel FeS cluster in Fe-only hydrogenases
Nicolet, Y., Lemon, B. J., Fontecilla-Camps, J. C., & Peters, J. W. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01536-4 · Cited by 417
Roseboom, W., De Lacey, A. L., Fernandez, V. M., Hatchikian, E. C., & Albracht, S. P. J. (2006) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-005-0040-2 · Cited by 261
Eukaryotic DNA polymerases, a growing family
Hübscher, U., Nasheuer, H.-P., & Syväoja, J. E. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01523-6 · Cited by 220
Electronic Structure of the H Cluster in [Fe]-Hydrogenases
Popescu, C. V., & Münck, E. (1999) · Journal of the American Chemical Society · doi:10.1021/ja991243y · Cited by 191
Reversible Carbon Monoxide Binding and Inhibition at the Active Site of the Fe-Only Hydrogenase
Bennett, B., Lemon, B. J., & Peters, J. W. (2000) · Biochemistry · doi:10.1021/bi992583z · Cited by 147
(1992) · Analytical Chemistry · doi:10.1021/ac00030a720 · Cited by 25
Cited by
N-Heterocyclic Carbenes in Late Transition Metal Catalysis
Díez-González, S., Marion, N., & Nolan, S. P. (2009) · Chemical Reviews · doi:10.1021/cr900074m · Cited by 3,066
Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO 2 Fixation
Appel, A. M., Bercaw, J. E., Bocarsly, A. B., Dobbek, H., DuBois, D. L., Dupuis, M., Ferry, J. G., Fujita, E., Hille, R., Kenis, P. J. A., et al. (2013) · Chemical Reviews · doi:10.1021/cr300463y · Cited by 2,193
Hydrogen Evolution Catalyzed by Cobaloximes
Dempsey, J. L., Brunschwig, B. S., Winkler, J. R., & Gray, H. B. (2009) · Accounts of Chemical Research · doi:10.1021/ar900253e · Cited by 1,070
Earth-abundant hydrogen evolution electrocatalysts
McKone, J. R., Marinescu, S. C., Brunschwig, B. S., Winkler, J. R., & Gray, H. B. (2014) · Chem. Sci. · doi:10.1039/c3sc51711j · Cited by 727
The Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site
Shima, S., Pilak, O., Vogt, S., Schick, M., Stagni, M. S., Meyer-Klaucke, W., Warkentin, E., Thauer, R. K., & Ermler, U. (2008) · Science · doi:10.1126/science.1158978 · Cited by 608
Metadata
- Authors
- Liu, T., & Darensbourg, M. Y.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-05-11
- Volume
- 129
- Issue
- 22
- Pages
- 7008-7009
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2072348323
- Cited by
- 300
- References
- 8
- FWCI
- 18.99
- Type
- journal article
- Language
- en
- Open access
- closed
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
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.