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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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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
Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods
Dias, J. M., Than, M. E., Humm, A., Huber, R., Bourenkov, G. P., Bartunik, H. D., Bursakov, S., Calvete, J., Caldeira, J., Carneiro, C., et al. (1999) · Structure · doi:10.1016/s0969-2126(99)80010-0 · Cited by 286
Self-citationCrystal Structure of Dimethyl Sulfoxide Reductase fromRhodobacter capsulatusat 1.88 Å Resolution
Schneider, F., Löwe, J., Huber, R., Schindelin, H., Kisker, C., & Knäblein, J. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0555 · Cited by 251
Architecture of NarGH Reveals a Structural Classification of Mo-bisMGD Enzymes
Jormakka, M., Richardson, D. J., Byrne, B., & Iwata, S. (2004) · Structure · doi:10.1016/j.str.2003.11.020 · Cited by 219
Truglio, J. J., Theis, K. W., Leimkühler, S., Rappa, R., Rajagopalan, K. V., & Kisker, C. (2002) · Structure · doi:10.1016/s0969-2126(01)00697-9 · Cited by 207
Raaijmakers, H. C. A., Macieira, S., Dias, J. M. L., Teixeira, S. C. M., Bursakov, S. A., Huber, R., Moura, J. J. G., Moura, I., & Romão, M. J. (2002) · Structure · doi:10.1016/s0969-2126(02)00826-2 · Cited by 194
Self-citationEvolution of Nitrate Reductase: Molecular and Structural Variations on a Common Function
Stolz, J. F., & Basu, P. (2002) · ChemBioChem · doi:10.1002/1439-7633(20020301)3:2/3 · Cited by 171
Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase
Arnoux, P., Sabaty, M., Alric, J., Frangioni, B., Guigliarelli, B., Adriano, J.-M., & Pignol, D. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb994 · Cited by 149
Khangulov, S. V., Gladyshev, V. N., Dismukes, G. C., & Stadtman, T. C. (1998) · Biochemistry · doi:10.1021/bi972177k · Cited by 144
Dissimilatory nitrate reductases in bacteria
Philippot, L., & Højberg, O. (1999) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(99)00072-x · Cited by 143
The coordination and function of the redox centres of the membrane-bound nitrate reductases
Blasco, F., Guigliarelli, B., Magalon, A., Asso, M., Giordano, G., & Rothery, R. A. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000846 · Cited by 117
de Bok, F. A. M., Hagedoorn, P., Silva, P. J., Hagen, W. R., Schiltz, E., Fritsche, K., & Stams, A. J. M. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03619.x · Cited by 116
Cytochrome c Nitrite Reductase from Desulfovibrio desulfuricans ATCC 27774
Cunha, C. A., Macieira, S., Dias, J. M. L., Almeida, G., Gonçalves, L. L., Costa, C., Lampreia, J., Huber, R., Moura, J. J. G., Moura, I., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211777200 · Cited by 109
Self-citationElectron-paramagnetic-resonance studies on nitrate reductase from Escherichia coli K12
Vincent, S. P., & Bray, R. C. (1978) · Biochemical Journal · doi:10.1042/bj1710639 · Cited by 106
The Reductive Half-reaction of Xanthine Oxidase
Xia, M., Dempski, R. E., & Hille, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.6.3323 · Cited by 99
Butler, C. S., Charnock, J. M., Bennett, B., Sears, H. J., Reilly, A. J., Ferguson, S. J., Garner, C. D., Lowe, D. J., Thomson, A. J., Berks, B. C., et al. (1999) · Biochemistry · doi:10.1021/bi990402n · Cited by 99
Stewart, L. J., Bailey, S., Bennett, B., Charnock, J., Garner, C. D., & McAlpine, A. S. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3702 · Cited by 95
Desulfovibrio alaskensis sp. nov., a sulphate-reducing bacterium from a soured oil reservoir
Feio, M. J. (2004) · INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY · doi:10.1099/ijs.0.63118-0 · Cited by 92
Buc, J., Santini, C., Giordani, R., Czjzek, M., Wu, L., & Giordano, G. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01340.x · Cited by 83
Costa, C., Teixeira, M. S., LeGall, J., Moura, J. J. G., & Moura, I. (1997) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050125 · Cited by 79
Self-citationMagalon, A., Asso, M., Guigliarelli, B., Rothery, R. A., Bertrand, P., Giordano, G., & Blasco, F. (1998) · Biochemistry · doi:10.1021/bi972858f · Cited by 78
Structure and function of molybdopterin containing enzymes
Romão, M. J., Knäblein, J., Huber, R., & Moura, J. J. G. (1997) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(97)00022-9 · Cited by 78
Self-citationAlmendra, M. J., Brondino, C. D., Gavel, O. Y., Pereira, A. S., Tavares, P., Bursakov, S. A., Duarte, R. O., Caldeira, J., Moura, J. J. G., & Moura, I. (1999) · Biochemistry · doi:10.1021/bi990069n · Cited by 76
Self-citationRichardson, D. J., & Sawers, R. G. (2002) · Science · doi:10.1126/science.1070366 · Cited by 75
Almeida, M. G., Macieira, S., Gonçalves, L. M. L., Huber, R., Cunha, C. A., Romão, M. J., Costa, C., Lampreia, J., Moura, J. J. G., & Moura, I. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03772.x · Cited by 71
Self-citationFrangioni, B., Arnoux, P., Sabaty, M., Pignol, D., Bertrand, P., Guigliarelli, B., & Léger, C. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0384072 · Cited by 70
Chemical keys to molybdenum enzymes *
Stiefel, E. I. (1997) · Journal of the Chemical Society Dalton Transactions · doi:10.1039/a704936f · Cited by 65
George, G. N., Bray, R. C., Morpeth, F. F., & Boxer, D. H. (1985) · Biochemical Journal · doi:10.1042/bj2270925 · Cited by 63
Brondino, C. D., Passeggi, M. C. G., Caldeira, J., Almendra, M. J., Feio, M. J., Moura, J. J. G., & Moura, I. (2003) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-003-0506-z · Cited by 61
Self-citationBursakov, S. A., Liu, M. Y., Payne, W. J., LeGall, J., Moura, I., & Moura, J. J. G. (1995) · Anaerobe · doi:10.1016/s1075-9964(95)80444-7 · Cited by 52
Self-citationRaaijmakers, H. C. A., Teixeira, S. C. M., Dias, J. M. L., Almendra, M. J., Brondino, C. D., Moura, I., Moura, J. J. G., & Romão, M. J. (2001) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750100215 · Cited by 48
Self-citationBrigé, A., Leys, D., Meyer, T. E., Cusanovich, M. A., & Van Beeumen, J. J. (2002) · Biochemistry · doi:10.1021/bi012144b · Cited by 47
Observation of Ligand-Based Redox Chemistry at the Active Site of a Molybdenum Enzyme
George, G. N., Costa, C., Moura, J. J. G., & Moura, I. (1999) · Journal of the American Chemical Society · doi:10.1021/ja9841761 · Cited by 44
Self-citationCopper‐containing nitrite reductase from Pseudomonas chlororaphis DSM 50135
Pinho, D., Besson, S., Brondino, C. D., de Castro, B., & Moura, I. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04155.x · Cited by 41
Self-citationThe bio-inorganic chemistry of tungsten
Hagen, W. R., & Arendsen, A. F. (1998) · Structure and bonding · doi:10.1007/3-540-62888-6_6 · Cited by 40
Redox reactions of the pyranopterin system of the molybdenum cofactor
Burgmayer, S. J. N., Pearsall, D. L., Blaney, S. M., Moore, E. M., & Sauk-Schubert, C. (2003) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-003-0496-x · Cited by 37
Hensgens, C. M. H., Hagen, W. R., & Hansen, T. A. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.21.6195-6200.1995 · Cited by 37
Butler, C. S., Fairhurst, S. A., Ferguson, S. J., THOMSON, A. J., Berks, B. C., RICHARDSON, D. J., & LOWE, D. J. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3630817 · Cited by 34
Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491
Andrade, S. L. A., Brondino, C. D., Feio, M. J., Moura, I., & Moura, J. J. G. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01209.x · Cited by 31
Self-citationGodfrey, C., Greenwood, C., THOMSON, A. J., Bray, R. C., & George, G. N. (1984) · Biochemical Journal · doi:10.1042/bj2240601 · Cited by 30
Brondino, C. D., Calvo, R., Atria, A. M., Spodine, E., Nascimento, O. R., & Peña, O. (1997) · Inorganic Chemistry · doi:10.1021/ic9610501 · Cited by 24
Self-citationHettmann, T., Siddiqui, R. A., von Langen, J., Frey, C., Romão, M. J., & Diekmann, S. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.08.114 · Cited by 24
Self-citationHettmann, T., Anemüller, S., Borcherding, H., Mathé, L., Steinrücke, P., & Diekmann, S. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03837-1 · Cited by 13
Molybdenum Enzymes in Reactions Involving Aldehydes and Acids
Romão, M. J., Cunha, C. A., Brondino, C. D., & Moura, J. J. G. (2002) · CRC Press eBooks · doi:10.1201/9780203909331-24 · Cited by 10
Self-citation
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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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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