The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Synthetic Analogues of the Active Sites of Iron−Sulfur Proteins
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSynthetic Analogues of the Active Sites of Iron−Sulfur ProteinsP. Venkateswara Rao and R. H. HolmView Author Information Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138 Cite this: Chem. Rev. 2004, 104, 2, 527–560Publication Date (Web):October 30, 2003Publication History Received17 March 2003Published online30 October 2003Published inissue 1 February 2004https://doi.org/10.1021/cr020615+Copyright © 2004 American Chemical SocietyRIGHTS & PERMISSIONSArticle Views6586Altmetric-Citations447LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit Read OnlinePDF (678 KB) Get e-AlertsSUBJECTS:Cluster chemistry,Metal clusters,Peptides and proteins,Protein structure,Redox reactions Get e-Alerts
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Citations
Cites
Shannon, R. D. (1976) · Acta Crystallographica Section A · doi:10.1107/s0567739476001551 · Cited by 66,145
Iron-sulfur clusters: nature's modular, multipurpose structures
Beinert, H., Holm, R. H., & Münck, E. (1997) · Science · doi:10.1126/science.277.5326.653 · Cited by 1,944
Self-citationAconitase as iron–sulfur protein, enzyme, and iron-regulatory protein
Beinert, H., Kennedy, M. C., & Stout, C. D. (1996) · Chemical Reviews · doi:10.1021/cr950040z · Cited by 606
Sulfite Reductase Structure at 1.6 Å: Evolution and Catalysis for Reduction of Inorganic Anions
Crane, B. R., Siegel, L. M., & Getzoff, E. D. (1995) · Science · doi:10.1126/science.270.5233.59 · Cited by 345
Cited by
Protein Design: Toward Functional Metalloenzymes
Yu, F., Cangelosi, V. M., Zastrow, M. L., Tegoni, M., Plegaria, J. S., Tebo, A. G., Mocny, C. S., Ruckthong, L., Qayyum, H., & Pecoraro, V. L. (2014) · Chemical Reviews · doi:10.1021/cr400458x · Cited by 441
Photochemical Nitrogen Conversion to Ammonia in Ambient Conditions with FeMoS-Chalcogels
Banerjee, A., Yuhas, B. D., Margulies, E. A., Zhang, Y., Shim, Y., Wasielewski, M. R., & Kanatzidis, M. G. (2015) · Journal of the American Chemical Society · doi:10.1021/ja512491v · Cited by 339
The Clusters of Nitrogenase: Synthetic Methodology in the Construction of Weak-Field Clusters
Lee, S. C., & Holm, R. H. (2004) · Chemical Reviews · doi:10.1021/cr0206216 · Cited by 313
Self-citationMammalian iron-sulphur proteins: novel insights into biogenesis and function
Rouault, T. A. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3909 · Cited by 201
UV-light-driven prebiotic synthesis of iron-sulfur clusters
Bonfio, C., Valer, L., Scintilla, S., Shah, S., Evans, D. J., Jin, L., Szostak, J. W., Sasselov, D. D., Sutherland, J. D., & Mansy, S. S. (2017) · Nature Chemistry · doi:10.1038/nchem.2817 · Cited by 158
Metadata
- Authors
- Venkateswara Rao, P., & Holm, R. H.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2003-10-30
- Volume
- 104
- Issue
- 2
- Pages
- 527-560
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2051509289
- Cited by
- 541
- References
- 4
- FWCI
- 2.11
- Type
- journal article
- Language
- en
- Open access
- closed
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