Cited by 1,738Metalloenzymes and iron-sulfur proteinsMetal-Catalyzed Oxygenation MechanismsEnzyme Structure and Function

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The Mononuclear Molybdenum Enzymes

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Hille, Russ, Hall, James, Basu, Partha·2014·Chemical Reviews

DOI 10.1021/cr400443zPMC PMC4080432

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ADVERTISEMENT RETURN TO ISSUEPREVReviewThe Mononuclear Molybdenum EnzymesRuss Hille*†, James Hall†, and Partha Basu*‡View Author Information† Department of Biochemistry, University of California, Riverside, Riverside, California 92521, United States‡ Department of Chemistry and Biochemistry, Duquesne University, Pittsburgh, Pennsylvania 15282, United States*E-mail: [email protected]*E-mail: [email protected]Cite this: Chem. Rev. 2014, 114, 7, 3963–4038Publication Date (Web):January 28, 2014Publication History Received13 August 2013Published online28 January 2014Published inissue 9 April 2014https://pubs.acs.org/doi/10.1021/cr400443zhttps://doi.org/10.1021/cr400443zreview-articleACS PublicationsCopyright © 2014 American Chemical SocietyRequest reuse permissionsArticle Views10413Altmetric-Citations493LEARN 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 InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Anions,Cluster chemistry,Molybdenum,Monomers,Peptides and proteins Get e-Alerts

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The Metabolic Basis of Inherited Disease.
(1988) · Annals of Internal Medicine · doi:10.7326/0003-4819-108-3-503_7 · Cited by 7,807
Oxygen-Derived Free Radicals in Postischemic Tissue Injury
Epstein, F. H., & McCord, J. M. (1985) · New England Journal of Medicine · doi:10.1056/nejm198501173120305 · Cited by 5,399
X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution
Peters, J. W. (1998) · Science · doi:10.1126/science.282.5395.1853 · Cited by 1,891
Natural engineering principles of electron tunnelling in biological oxidation–reduction
Page, C. C., Moser, C. C., Chen, X., & Dutton, P. L. (1999) · Nature · doi:10.1038/46972 · Cited by 1,866
Mechanism of Molybdenum Nitrogenase
Burgess, B. K., & Lowe, D. J. (1996) · Chemical Reviews · doi:10.1021/cr950055x · Cited by 1,854
Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas
Volbeda, A., Charon, M., Piras, C., Hatchikian, E. C., Frey, M., & Fontecilla-Camps, J. C. (1995) · Nature · doi:10.1038/373580a0 · Cited by 1,573
The Mononuclear Molybdenum Enzymes
Hille, R. (1996) · Chemical Reviews · doi:10.1021/cr950061t · Cited by 1,501
Self-citation
ABC transporters: the power to change
Rees, D. C., Johnson, E., & Lewinson, O. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2646 · Cited by 1,454
Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex
Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., & Jap, B. K. (1998) · Science · doi:10.1126/science.281.5373.64 · Cited by 1,253
Structural basis of biological nitrogen fixation
Rees, D. C., Tezcan, F. A., Haynes, C. A., Walton, M. Y., Andrade, S. L. A., Einsle, O., & Howard, J. B. (2005) · Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences · doi:10.1098/rsta.2004.1539 · Cited by 1,128

Show all 1,038 references

Research works printed but not linked: 26

Kirk M. L., 2004, Prog. Inorg. Chem., 52, 111
Leimkuhler S., 2011, Coord. Chem. Rev., 255, 1129, 10.1016/j.ccr.2010.12.003 · DOI
Unden G., 2002, J. Mol. Microbiol. Biotechnol., 4, 263
Fischer K., 2006, J. Biol. Chem., 281, 30186, 10.1074/jbc.m603919200 · DOI
Iobbi-Nivol C., 2013, Biochim. Biophys. Acta, 1827, 1086, 10.1016/j.bbabio.2012.11.007 · DOI
Lim L. W., 1986, J. Biol. Chem., 261, 5140
Godber B. L. J., 2001, Biochem. J., 358, 325, 10.1042/bj3580325 · DOI
Neumann M., 2009, J. Biol. Chem., 284, 21891, 10.1074/jbc.m109.008565 · DOI
Pauff J. M., 2007, J. Biol. Chem., 282, 12785, 10.1074/jbc.m700364200 · DOI
Meyer O., 1993, Microb. Growth C1 Compd., 27
Moersdorf G., 1992, Biodegradation, 3, 61
Meyer-Klaucke W., 2001, J. Inorg. Biochem., 86, 339
Wilcoxen J., 2013, J. Biol. Chem., 288
bGladyshev, V. N.Molybdenum and Tungsten: Their Roles in Biological Processes;CRC Press:New York, 2002; Vol.39, p655.
Gladyshev V. N., 1995, BioFactors, 5, 93
Klein J. M., 2012, J. Cell Sci., 125, 4876
George G. N., 1985, J. Magn. Reson., 64, 384
Cohen H. J., 1972, Fed. Proc., 31, 850
Bachmann M., 1996, Plant Cell, 8, 505
Kotthaus J., 2011, Biochem. J., 433, 383, 10.1042/bj20100960 · DOI · Paper page
Anantharaman V., 2002, FEMS Microbiol. Lett., 207, 55
Rothery R. A., 2002, J. Mol. Microbiol. Biotechnol., 4, 133
Graham N., 2007, Inorg. Chem., 46, 2, 10.1021/ic061695t · DOI
Dong Y. Y., 2012, PLoS One, 7
Butler C. S., 2002, Biochem. J., 363, 817, 10.1042/bj3630817 · DOI
Gates A. J., 2011, Biochem. J., 435, 743, 10.1042/bj20101920 · DOI

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Self-citation
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Mohr, M., McNamara, J. P., Wang, H., Rajeev, S. A., Ge, J., Morgado, C. A., & Hillier, I. H. (2003) · Faraday Discussions · doi:10.1039/b211791f · Cited by 44
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Authors: Hille, R., Hall, J., & Basu, P.
Affiliations: University of California, Riverside (US)
Duquesne University (US)
Corresponding author: Hille, Russ
Basu, Partha
ORCID: Hille, Russ
Hall, James
Basu, Partha
Venue: Chemical Reviews
Publisher: American Chemical Society (ACS)
Published: 2014-01-28
Volume: 114
Issue: 7
Pages: 3963-4038
ISSN: 0009-2665 (ISSN-L)
1520-6890
DOI: 10.1021/cr400443z
PMC: PMC4080432
OpenAlex: W2045245826
Cited by: 1,738
References: 1,038
Citations by year: 2026: 41 · 2025: 55 · 2024: 64 · 2023: 65 · 2022: 63 · 2021: 79 · 2020: 72 · 2019: 65 · 2018: 70 · 2017: 69 · 2016: 77 · 2015: 72 · 2014: 80
FWCI: 3.75
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Chemical Reviews (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of General Medical Sciences (R15GM061555)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: molybdenum enzymes, molybdenum clusters, molybdenum cofactor, enzyme active site, metalloproteins, metalloenzymes
MeSH terms: Aldehyde Oxidoreductases, Formate Dehydrogenases, Iron-Sulfur Proteins, Molybdenum, Nitrate Reductases, Oxidoreductases, Xanthine Oxidase, Protein Structure, Tertiary, Sulfite Oxidase, Biocatalysis

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