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.
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“the extra residues are distributed over themolecular surface.187”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [187]
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
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
Flagged first, then by citations
1 of the 54 references couldn’t be matched to a known paper.
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
Cited by
Sorted by citations
Items 101–141 of 141
EPR Spectroscopy on Mononuclear Molybdenum-Containing Enzymes
Maia, L. B., Moura, I., & Moura, J. J. G. (2017) · Biological magnetic resonance · doi:10.1007/978-3-319-59100-1_4 · Cited by 11
Self-citationBudhraja, R., Ding, C., Walter, P., Wagner, S., Reemtsma, T., Sawers, R. G., & Adrian, L. (2019) · Metallomics · doi:10.1039/c9mt00009g · Cited by 11
O-Atom Exchange between H2O and CO2 Mediated by a Bis(dithiolene)tungsten Complex
Seo, J., & Kim, E. (2012) · Inorganic Chemistry · doi:10.1021/ic300906j · Cited by 10
Maeda, Y., Doubayashi, D., Ootake, T., Oki, M., Mikami, B., & Uchida, H. (2010) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309110028605 · Cited by 9
Structural Biology of Fungal Multicopper Oxidases
Enguita, F. J. (2011) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/978160805223311101010057 · Cited by 9
Molybdenum and Tungsten Oxidoreductase Models
Schulzke, C., & Ghosh, A. C. (2014) · Wiley eBooks · doi:10.1002/9783527664160.ch13 · Cited by 9
Zhu, X., Gu, X., Zhang, S., Liu, Y., Huang, Z., & Tan, X. (2011) · Protein Expression and Purification · doi:10.1016/j.pep.2011.02.006 · Cited by 8
An Introduction to the Role of Molybdenum and Tungsten in Biology
Marques, H. M. (2025) · Inorganics · doi:10.3390/inorganics13070219 · Cited by 9
Alavi-Borazjani, S. A., Gomes, H. G. M. F., Tarelho, L. A. C., & Capela, M. I. (2023) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-023-02873-6 · Cited by 6
Wei, Y., Zhu, X., Zhang, S., & Tan, X. (2017) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2017.02.005 · Cited by 6
Ferroni, F. M., Rivas, M. G., Rizzi, A. C., Lucca, M. E., Perotti, N. I., & Brondino, C. D. (2011) · BioMetals · doi:10.1007/s10534-011-9442-5 · Cited by 6
Self-citationLi, F., & Lienemann, M. (2025) · FEBS Journal · doi:10.1111/febs.70048 · Cited by 5
Molecular modulation of NiFe hydrogenase activity
Dementin, S., Belle, V., Champ, S., Bertrand, P., Guigliarelli, B., Lacey, A. L. D., Fernández, V. M., Léger, C., & Rousset, M. (2007) · International Journal of Hydrogen Energy · doi:10.1016/j.ijhydene.2007.09.046 · Cited by 5
Biomimetic Applications of Metal Systems Supported by Scorpionates
Pellei, M., & Santini, C. (2011) · InTech eBooks · doi:10.5772/14854 · Cited by 6
The Green Alga Chlamydomonas as a Tool to Study the Nitrate Assimilation Pathway in Plants
Mariscal, V., Fernández, E. M., González-Ballester, D., & Galván, A. (2006) · CRC Press eBooks · doi:10.1201/9780849330636.ch7 · Cited by 5
Amelioration of enteric dysbiosis by polyoxotungstates in mice gut
Chen, K., Liu, Y., Li, M., Liu, L., Yu, Q., & Wu, L. B. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111654 · Cited by 4
Mononuclear Molybdenum-Containing Enzymes
Maia, L. B., & Moura, J. J. G. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.13932-0 · Cited by 4
Self-citationBiological Methods for Carbon Dioxide Conversion and Utilization
Saqib, S., Mukhtar, A., Ullah, S., Sagir, M., Tahir, M. B., Amen, R., Babar, M., Al-Sehemi, A. G., Assiri, M. A., & Ibrahim, M. (2021) · Advances in Science, Technology & Innovation/Advances in science, technology & innovation · doi:10.1007/978-3-030-61837-7_10 · Cited by 3
How Many Microorganisms Are Present? Quantitative Reverse Transcription PCR (qRT-PCR)
Price, A., Álvarez, L. A., Whitby, C. B., & Larsen, J. O. (2010) · Springer eBooks · doi:10.1007/978-90-481-9252-6_9 · Cited by 3
The Green Alga Chlamydomonas as a Tool to Study the Nitrate Assimilation Pathway in Plants
Mariscal, V., Fernández, E. M., González-Ballester, D., & Galván, A. (2006) · CRC Press eBooks · doi:10.1201/9781420004618.ch7 · Cited by 3
Tejada‐Jiménez, M., & Schwarz, G. (2014) · Royal Society of Chemistry eBooks · doi:10.1039/9781849739979-00223 · Cited by 2
Selenocysteine-dependent Enzymes: Structure, Function and Selenium-derived Mechanism
Li, F., Gao, J., & Zhang, Y. (2026) · Journal of Molecular Biology · doi:10.1016/j.jmb.2026.169771 · Cited by 1
Formate metabolism in sulfate reducing bacteria
da Silva, S. M. (2011) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
The Membrane‐Bound Nitrate Reductase A from Escherichia Coli: Nar GHI
Bertero, M. G. (2004) · Handbook of Metalloproteins · doi:10.1002/0470028637.met235
Sulemankhil, I. (2013) · eScholarship@McGill (McGill) · doi:10.82308/52531
Characterization of molybdenum and tungsten formate dehydrogenases from sulfate reducing bacteria
Mota, C. (2011) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
Catalysis of CO2 Electroreduction
Chen, R., & Liu, Y. (2016) · Electrochemical energy storage and conversion · doi:10.1201/b20177-5
Wei, Y., & Tan, X. (2017) · Chemical Research in Chinese Universities · doi:10.1007/s40242-017-7142-6
Ge, X., Thorgersen, M. P., Poole, F. L., Deutschbauer, A. M., Chandonia, J., Novichkov, P. S., Adams, P. D., Arkin, A. P., Hazen, T. C., & Adams, M. W. W. (2020) · Microbiology Resource Announcements · doi:10.1128/mra.01149-20
He, S., An, Y., Yang, H., Cao, R., Tang, Q., & Wang, L. (2020) · doi:10.21203/rs.3.rs-74929/v1
Liu, M., Nazemi, A., Taylor, M. G., Nandy, A., Duan, C., Steeves, A. H., & Kulik, H. J. (2021) · doi:10.33774/chemrxiv-2021-397ph
The Membrane‐Bound Nitrate Reductase A from Escherichia Coli: Nar GHI
Bertero, M. G. (2011) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc0661
Valorisation of Carbon Dioxide via Enzymatic Transformation
Meyer, A. S. (2022) · Royal Society of Chemistry eBooks · doi:10.1039/9781839167645-00486
Lenkennavar, S. K. (2023) · Journal of Condensed Matter · doi:10.61343/jcm.v1i02.31
Computational studies on oxidative mechanism of nirtrate reductase
Periyasamy, G., & Lenkennavar, S. K. (2024) · AIP conference proceedings · doi:10.1063/5.0228894
One Hundred Years of Sulfido Ligand in the Molybdenum Cofactor: New Perspectives
Leimkühler, S., Duffus, B. R., & Schulzke, C. (2026) · ChemBioChem · doi:10.1002/cbic.70527
Oxygen-sensitive mechanisms and protective strategies of metalloenzymes
Li, F., Wang, J., Li, R., & Gao, J. (2026) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2026.113473
Perchlorate reduction using Azospira oryzae enzymes in synthetic vesicles
Hutchison, J. M. (2012) · Illinois Digital Environment for Access to Learning and Scholarship (University of Illinois at Urbana-Champaign)
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
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