The DOI matches its Crossref record; 53 of the 54 references it cites were found in a registry or an index.
Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases
Open accessAbstract
Molybdenum and tungsten are second- and third-row transition elements, respectively, which are found in a mononuclear form in the active site of a diverse group of enzymes that generally catalyze oxygen atom transfer reactions. Mononuclear Mo-containing enzymes have been classified into three families: xanthine oxidase, DMSO reductase, and sulfite oxidase. The proteins of the DMSO reductase family present the widest diversity of properties among its members and our knowledge about this family was greatly broadened by the study of the enzymes nitrate reductase and formate dehydrogenase, obtained from different sources. We discuss in this review the information of the better characterized examples of these two types of Mo enzymes and W enzymes closely related to the members of the DMSO reductase family. We briefly summarize, also, the few cases reported so far for enzymes that can function either with Mo or W at their active site.
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The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738
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
Boyington, J. C., Gladyshev, V. N., Khangulov, S. V., Stadtman, T. C., & Sun, P. D. (1997) · Science · doi:10.1126/science.275.5304.1305 · Cited by 596
Electron-Tunneling Pathways in Oroteins
Beratan, D. N., Onuchic, J. N., Winkler, J. R., & Gray, H. B. (1992) · Science · doi:10.1126/science.1334572 · Cited by 522
MOLYBDENUM-COFACTOR–CONTAINING ENZYMES: Structure and Mechanism
Kisker, C., Schindelin, H., & Rees, D. C. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.233 · Cited by 519
Molecular Basis of Proton Motive Force Generation: Structure of Formate Dehydrogenase-N
Jormakka, M., Törnroth‐Horsefield, S., Byrne, B., & Iwata, S. (2002) · Science · doi:10.1126/science.1068186 · Cited by 502
Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A
Bertero, M. G., Rothery, R. A., Palak, M., Hou, C., Lim, D., Blasco, F., Weiner, J. H., & Strynadka, N. C. J. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb969 · Cited by 494
Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination
Schindelin, H., Kisker, C., Hilton, J. C., Rajagopalan, K. V., & Rees, D. C. (1996) · Science · doi:10.1126/science.272.5268.1615 · Cited by 455
Johnson, M. K., Rees, D. C., & Adams, M. W. W. (1996) · Chemical Reviews · doi:10.1021/cr950063d · Cited by 324
Research works printed but not linked: 3
- Romao MJ, Cunha CA, Brondino CD, Moura JJ (2002) Met Ions Biol Syst 39:539?570
- Basu P, Stolz JF, Smith T (2003) Curr Sci 84:1412?1418
- Butler CS, Fairhurst SA, Ferguson SJ, Thomson AJ, Berks BC, Richardson DJ, Lowe DJ (2002) Biochem J 363:817?23 · DOI
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Nitrate and periplasmic nitrate reductases
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Metadata
- Authors
- Moura, J. J. G., Brondino, C. D., Trinc�o, J., & Rom�o, M. J.
- Affiliations
- Universidad Nacional del Litoral (AR)
- Universidade Nova de Lisboa (PT)
- ORCID
- Brondino, Carlos D.
- Venue
- JBIC Journal of Biological Inorganic Chemistry
- Published
- 2004-08-12
- Volume
- 9
- Issue
- 7
- Pages
- 791-799
- ISSN
- 0949-8257 (ISSN-L)
- 1432-1327
- OpenAlex
- W2042816956
- Cited by
- 141
- References
- 54
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 2 · 2023: 3 · 2022: 5 · 2021: 4 · 2020: 5 · 2019: 2 · 2018: 6 · 2017: 7 · 2016: 4 · 2015: 4 · 2014: 9 · 2013: 6 · 2012: 12
- FWCI
- 1.31
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- other-oa
- www.springer.com/tdm (tdm)
- Locations
- JBIC Journal of Biological Inorganic Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, other-oa)
- 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, tungsten enzymes, nitrate reductase, formate dehydrogenase, sulfite oxidase, xanthine oxidase, oxygen atom transfer, enzyme active site, metalloenzyme catalysis
- MeSH terms
- Electron Transport, Formate Dehydrogenases, Molybdenum, Nitrate Reductases, Tungsten, Nitrate Reductase
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