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
A review of catalysts for the electroreduction of carbon dioxide to produce low-carbon fuels
Qiao, J., Liu, Y., Hong, F., & Zhang, J. (2014) · Chem. Soc. Rev. · doi:10.1039/c3cs60323g · Cited by 2,990
Utilisation of CO2 as a chemical feedstock: opportunities and challenges
Aresta, M., & Dibenedetto, A. (2007) · Dalton Transactions · doi:10.1039/b700658f · Cited by 1,454
Molybdenum cofactors, enzymes and pathways
Schwarz, G., Mendel, R. R., & Ribbe, M. W. (2009) · Nature · doi:10.1038/nature08302 · Cited by 872
Direct Electrochemistry of Redox Enzymes as a Tool for Mechanistic Studies
Léger, C., & Bertrand, P. (2008) · Chemical Reviews · doi:10.1021/cr0680742 · Cited by 802
Nitrate and periplasmic nitrate reductases
Sparacino-Watkins, C., Stolz, J. F., & Basu, P. (2014) · Chem. Soc. Rev. · doi:10.1039/c3cs60249d · Cited by 426
Trace metal metabolism in plants
Andresen, E., Peiter, E., & Küpper, H. (2018) · Journal of Experimental Botany · doi:10.1093/jxb/erx465 · Cited by 431
Bacterial nitrate reductases: Molecular and biological aspects of nitrate reduction
González, P. J., Correia, C., Moura, I., Brondino, C. D., & Moura, J. J. G. (2006) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2005.11.024 · Cited by 285
Self-citationAnammox—Growth Physiology, Cell Biology, and Metabolism
Kartal, B., van Niftrik, L., Keltjens, J. T., den Camp, H. J. M. O., & Jetten, M. S. M. (2012) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/b978-0-12-398264-3.00003-6 · Cited by 273
Applications of oxidoreductases: Recent progress
Xu, F. (2005) · Industrial Biotechnology · doi:10.1089/ind.2005.1.38 · Cited by 229
The prokaryotic complex iron–sulfur molybdoenzyme family
Rothery, R. A., Workun, G. J., & Weiner, J. H. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.09.002 · Cited by 228
Stripp, S. T., Duffus, B. R., Fourmond, V., Léger, C., Leimkühler, S., Hirota, S., Hu, Y., Jasniewski, A. J., Ogata, H., & Ribbe, M. W. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00914 · Cited by 229
Soil Contamination, Nutritive Value, and Human Health Risk Assessment of Heavy Metals: An Overview
Oves, M., Khan, M. S., Zaidi, A., & Ahmad, E. (2012) · Springer eBooks · doi:10.1007/978-3-7091-0730-0_1 · Cited by 186
Molybdenum and tungsten enzymes: a crystallographic and mechanistic overview
Romão, M. J. (2009) · Dalton Transactions · doi:10.1039/b821108f · Cited by 187
Self-citationThe bioinorganic chemistry of tungsten
Bevers, L. E., Hagedoorn, P., & Hagen, W. R. (2008) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2008.01.017 · Cited by 171
Raaijmakers, H. C. A., & Romão, M. J. (2006) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-006-0129-2 · Cited by 174
Self-citationMolybdenum and tungsten-dependent formate dehydrogenases
Maia, L. B., Moura, J. J. G., & Moura, I. (2014) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-014-1218-2 · Cited by 164
Self-citationMolybdenum cofactor biosynthesis and deficiency
Schwarz, G. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5269-y · Cited by 164
Hartmann, T., & Leimkühler, S. (2013) · FEBS Journal · doi:10.1111/febs.12528 · Cited by 161
Jewell, T., Karaöz, U., Brodie, E., Williams, K. H., & Beller, H. R. (2016) · The ISME Journal · doi:10.1038/ismej.2016.25 · Cited by 137
Toward the Mechanistic Understanding of Enzymatic CO2 Reduction
Oliveira, A. R., Mota, C., Mourato, C., Domingos, R. M., Santos, M. F. A., Gesto, D., Guigliarelli, B., Santos‐Silva, T., Romão, M. J., & Pereira, I. A. C. (2020) · ACS Catalysis · doi:10.1021/acscatal.0c00086 · Cited by 141
Self-citationBlum, J., Su, Q., Ma, Y., Valverde‐Pérez, B., Domingo‐Félez, C., Jensen, M. M., & Smets, B. F. (2018) · Environmental Microbiology · doi:10.1111/1462-2920.14063 · Cited by 135
Genomic View of Energy Metabolism in Ralstonia eutropha H16
Cramm, R. (2008) · Microbial Physiology · doi:10.1159/000142893 · Cited by 133
Najmudin, S., González, P. J., Trincão, J., Coelho, C., Mukhopadhyay, A., Cerqueira, N. M. F. S. A., Romão, C. C., Moura, I., Moura, J. J. G., Brondino, C. D., et al. (2008) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-008-0359-6 · Cited by 116
Self-citationMolybdenum enzymes in bacteria and their maturation
Magalon, A., Fedor, J. G., Walburger, A., & Weiner, J. H. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.12.031 · Cited by 120
Fogeron, T., Todorova, T. K., Porcher, J., Gómez-Mingot, M., Chamoreau, L., Mellot‐Draznieks, C., Li, Y., & Fontecave, M. (2018) · ACS Catalysis · doi:10.1021/acscatal.7b03383 · Cited by 114
Molybdenum and tungsten enzymes: the xanthine oxidase family
Brondino, C. D., Romão, M. J., Moura, I., & Moura, J. J. G. (2006) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2006.01.034 · Cited by 111
Self-citationMarpani, F., Pinelo, M., & Meyer, A. S. (2017) · Biochemical Engineering Journal · doi:10.1016/j.bej.2017.08.011 · Cited by 106
Assembly and catalysis of molybdenum or tungsten-containing formate dehydrogenases from bacteria
Hartmann, T., Schwanhold, N., & Leimkühler, S. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.12.006 · Cited by 99
Coelho, C., González, P. J., Moura, J. G., Moura, I., Trincão, J., & João Romão, M. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.03.016 · Cited by 97
Self-citationThe mechanism of formate oxidation by metal-dependent formate dehydrogenases
Mota, C., Rivas, M. G., Brondino, C. D., Moura, I., Moura, J. J. G., González, P. J., & Cerqueira, N. M. F. S. A. (2011) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-011-0813-8 · Cited by 96
Self-citationReduction of molybdate by sulfate-reducing bacteria
Biswas, K. C., Woodards, N. A., Xu, H., & Barton, L. L. (2009) · BioMetals · doi:10.1007/s10534-008-9198-8 · Cited by 96
Guiral, M., Infossi, P., Aubert, C., Gloter, A., Iobbi‐Nivol, C., & Giudici‐Orticoni, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508034200 · Cited by 102
Tungsten, the Surprisingly Positively Acting Heavy Metal Element for Prokaryotes
Andreesen, J. R., & Makdessi, K. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1419.003 · Cited by 94
Simpson, P. J. L., Richardson, D. J., & Codd, R. (2009) · Microbiology · doi:10.1099/mic.0.034421-0 · Cited by 79
da Silva, S. M., Pimentel, C., Valente, F. M. A., Rodrigues‐Pousada, C., & Pereira, I. A. C. (2011) · Journal of Bacteriology · doi:10.1128/jb.00042-11 · Cited by 78
Structural aspects of mononuclear Mo/W-enzymes
Dobbek, H. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.11.017 · Cited by 78
Brokx, S. J., Rothery, R. A., Zhang, G., Ng, D. P., & Weiner, J. H. (2005) · Biochemistry · doi:10.1021/bi050621a · Cited by 74
Hartmann, T., Schrapers, P., Utesch, T., Nimtz, M., Rippers, Y., Dau, H., Mroginski, M. A., Haumann, M., & Leimkühler, S. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00002 · Cited by 70
Zerkle, A. L., Scheiderich, K., Maresca, J. A., Liermann, L. J., & Brantley, S. L. (2010) · Geobiology · doi:10.1111/j.1472-4669.2010.00262.x · Cited by 71
Cerqueira, N. M. F. S. A., Fernandes, P. A., González, P. J., Moura, J. J. G., & Ramos, M. J. (2013) · Inorganic Chemistry · doi:10.1021/ic3028034 · Cited by 64
Self-citationMolybdenum and Tungsten Oxidoreductase Models
Schulzke, C. (2011) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201001036 · Cited by 61
Assessment of DFT Methods for Computing Activation Energies of Mo/W-Mediated Reactions
Hu, L., & Chen, H. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5b00373 · Cited by 59
Oxo-molybdenum and oxo-tungsten complexes of Schiff bases relevant to molybdoenzymes
Lyashenko, G., Saischek, G., Judmaier, M. E., Volpe, M., Baumgartner, J., Belaj, F., Jančík, V., Herbst‐Irmer, R., & Zanetti, N. C. (2009) · Dalton Transactions · doi:10.1039/b820629e · Cited by 57
The effect of the sixth sulfur ligand in the catalytic mechanism of periplasmic nitrate reductase
Cerqueira, N. M. F. S. A., Gonzalez, P. J., Brondino, C. D., Romão, M. J., Romão, C. C., Moura, I., & Moura, J. J. G. (2009) · Journal of Computational Chemistry · doi:10.1002/jcc.21280 · Cited by 56
Self-citationSmeltz, J. L., Lilly, C. P., Boyle, P. D., & Ison, E. A. (2013) · Journal of the American Chemical Society · doi:10.1021/ja401390v · Cited by 54
Tungstoenzymes: Occurrence, Catalytic Diversity and Cofactor Synthesis
Seelmann, C. S., Willistein, M., Heider, J., & Boll, M. (2020) · Inorganics · doi:10.3390/inorganics8080044 · Cited by 56
Enzymatic carbon dioxide to formate: Mechanisms, challenges and opportunities
Chen, H., Huang, Y., Sha, C., Moradian, J. M., Yong, Y., & Fang, Z. (2023) · Renewable and Sustainable Energy Reviews · doi:10.1016/j.rser.2023.113271 · Cited by 51
Molybdenum Availability Is Key to Nitrate Removal in Contaminated Groundwater Environments
Thorgersen, M. P., Lancaster, W. A., Vaccaro, B. J., Poole, F. L., Rocha, A. M., Mehlhorn, T. L., Pettenato, A., Ray, J., Waters, R. J., Melnyk, R. A., et al. (2015) · Applied and Environmental Microbiology · doi:10.1128/aem.00917-15 · Cited by 51
Rivas, M. G., González, P. J., Brondino, C. D., Moura, J. J. G., & Moura, I. (2007) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2007.04.011 · Cited by 52
Self-citationBrondino, C. D., Rivas, M. G., Romão, M. J., Moura, J. J. G., & Moura, I. (2006) · Accounts of Chemical Research · doi:10.1021/ar050104k · Cited by 50
Self-citationJang, J., Jeon, B. W., & Kim, Y. H. (2018) · Scientific Reports · doi:10.1038/s41598-018-23924-z · Cited by 45
Rothery, R. A., Bertero, M. G., Spreter, T., Bouromand, N., Strynadka, N. C. J., & Weiner, J. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.066027 · Cited by 49
Bertrand, P., Frangioni, B., Dementin, S., Sabaty, M., Arnoux, P., Guigliarelli, B., Pignol, D., & Léger, C. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp074340j · Cited by 45
González, P. J., Rivas, M. G., Brondino, C. D., Bursakov, S. A., Moura, I., & Moura, J. J. G. (2006) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-006-0110-0 · Cited by 45
Self-citationGonzález, P. J., Rivas, M. G., Mota, C., Brondino, C. D., Moura, I., & Moura, J. J. G. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.05.020 · Cited by 45
Self-citationMota, C., Valette, O., González, P. J., Brondino, C. D., Moura, J. J. G., Moura, I., Dolla, A. R., & Rivas, M. G. (2011) · Journal of Bacteriology · doi:10.1128/jb.01531-10 · Cited by 43
Self-citationMarangon, J., Paes de Sousa, P. M., Moura, I., Brondino, C. D., Moura, J. J. G., & González, P. J. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.04.011 · Cited by 40
Self-citationBiaso, F., Burlat, B., & Guigliarelli, B. (2012) · Inorganic Chemistry · doi:10.1021/ic201533p · Cited by 40
Shifting the metallocentric molybdoenzyme paradigm: the importance of pyranopterin coordination
Rothery, R. A., & Weiner, J. H. (2014) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-014-1194-6 · Cited by 42
Evidence for the Formation of a Mo–H Intermediate in the Catalytic Cycle of Formate Dehydrogenase
Tiberti, M., Papaleo, E., Russo, N., GIOIA, L. D., & Zampella, G. (2012) · Inorganic Chemistry · doi:10.1021/ic300863d · Cited by 40
Volpe, M., & Zanetti, N. C. (2012) · Inorganic Chemistry · doi:10.1021/ic201681u · Cited by 39
Nitrogen Assimilation and its Regulation
Fernández, E. M., Llamas, Á., & Galván, A. (2009) · Elsevier eBooks · doi:10.1016/b978-0-12-370873-1.00011-3 · Cited by 39
Majumdar, A. (2014) · Dalton Transactions · doi:10.1039/c4dt00631c · Cited by 39
Reimann, J., Jetten, M., & Keltjens, J. (2015) · Metal ions in life sciences · doi:10.1007/978-3-319-12415-5_7 · Cited by 27
Reassessing the Strategies for Trapping Catalytic Intermediates during Nitrate Reductase Turnover
Fourmond, V., Sabaty, M., Arnoux, P., Bertrand, P., Pignol, D., & Léger, C. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp911443y · Cited by 33
Transformations of Dimethylsulfide
Kappler, U., & Schäfer, H. (2014) · Metal ions in life sciences · doi:10.1007/978-94-017-9269-1_11 · Cited by 31
Acetylene hydratase: a non-redox enzyme with tungsten and iron–sulfur centers at the active site
Kroneck, P. M. H. (2016) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-015-1330-y · Cited by 32
Maiti, B. K., Almeida, R. M., Moura, I., & Moura, J. J. G. (2017) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2017.10.001 · Cited by 35
Self-citationde Vries, S., Momcilovic, M., Strampraad, M. J. F., Whitelegge, J. P., Baghai, A., & Schröder, I. (2010) · Biochemistry · doi:10.1021/bi100974v · Cited by 29
Nitrate and (per)chlorate reduction pathways in (per)chlorate-reducing bacteria
Oosterkamp, M. J., Mehboob, F., Schraa, G., Plugge, C. M., & Stams, A. J. M. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390230 · Cited by 29
Hofmann, M. (2007) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-007-0271-5 · Cited by 30
Thapper, A., Behrens, A., Fryxelius, J., Johansson, M. H., Prestopino, F., Czaun, M., Rehder, D., & Nordlander, E. (2005) · Dalton Transactions · doi:10.1039/b505180k · Cited by 31
Molybdate and Tungstate: Uptake, Homeostasis, Cofactors, and Enzymes
Schwarz, G., Hagedoorn, P., & Fischer, K. (2007) · Springer eBooks · doi:10.1007/7171_2006_088 · Cited by 30
Fourmond, V., Burlat, B., Dementin, S., Sabaty, M., Arnoux, P., Étienne, É., Guigliarelli, B., Bertrand, P., Pignol, D., & Léger, C. (2010) · Biochemistry · doi:10.1021/bi902140e · Cited by 28
Rivas, M. G., Carepo, M. S. P., Mota, C., Korbas, M., Durand, M.-C., Lopes, A. T., Brondino, C. D., Pereira, A. S., George, G. N., Dolla, A. R., et al. (2009) · Biochemistry · doi:10.1021/bi801773t · Cited by 27
Self-citationCorreia, C., Besson, S., Brondino, C. D., González, P. J., Fauque, G. D., Lampreia, J., Moura, I., & Moura, J. J. G. (2008) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-008-0416-1 · Cited by 30
Self-citationPyranopterin Coordination Controls Molybdenum Electrochemistry in Escherichia coli Nitrate Reductase
Wu, S.-Y., Rothery, R. A., & Weiner, J. H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.665422 · Cited by 27
Theoretical studies on mechanisms of some Mo enzymes
Cerqueira, N. M. F. S. A., Pakhira, B., & Sarkar, S. (2015) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-015-1237-7 · Cited by 26
Höschle, B., & Jendrossek, D. (2005) · Microbiology · doi:10.1099/mic.0.27957-0 · Cited by 26
Ge, X., Vaccaro, B. J., Thorgersen, M. P., Poole, F. L., Majumder, E. L. ‐., Zane, G. M., León, K. B. D., Lancaster, W. A., Moon, J., Paradis, C. J., et al. (2018) · Environmental Microbiology · doi:10.1111/1462-2920.14435 · Cited by 25
Dissimilatory nitrate and nitrite ammonification by sulphate-reducing eubacteria
Moura, J. J. G., González, P. J., Moura, I., & Fauque, G. D. (2007) · Cambridge University Press eBooks · doi:10.1017/cbo9780511541490.009 · Cited by 28
Self-citationWitthoff, S., Eggeling, L., Bott, M. H., & Polen, T. (2012) · Microbiology · doi:10.1099/mic.0.059196-0 · Cited by 25
Inspired by Nature—Functional Analogues of Molybdenum and Tungsten-Dependent Oxidoreductases
Pätsch, S., Correia, J. V., Elvers, B. J., Steuer, M., & Schulzke, C. (2022) · Molecules · doi:10.3390/molecules27123695 · Cited by 21
Ge, X., Thorgersen, M. P., Poole, F. L., Deutschbauer, A. M., Chandonia, J., Novichkov, P. S., Gushgari-Doyle, S., Lui, L. M., Nielsen, T., Chakraborty, R., et al. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.587127 · Cited by 21
Simpson, P. J. L., McKinzie, A. A., & Codd, R. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.06.002 · Cited by 20
Nanobiocatalysts for Carbon Capture, Sequestration and Valorisation
Rayalu, S. S., Yadav, R., Wanjari, S., Prabhu, C., Mushnoori, S., Labhsetwar, N. K., Satyanarayanan, T., Kotwal, S. D., Wate, S. R., Hong, S.-G., et al. (2012) · Topics in Catalysis · doi:10.1007/s11244-012-9896-x · Cited by 20
Faster oxygen atom transfer catalysis with a tungsten dioxo complex than with its molybdenum analog
Arumuganathan, T., Mayilmurugan, R., Volpe, M., & Zanetti, N. C. (2011) · Dalton Transactions · doi:10.1039/c1dt10248f · Cited by 19
Simpson, P. J. L., & Codd, R. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.10.003 · Cited by 17
Chemistry and Relevant Biomimetic Applications of Group 6 Metals Systems Supported by Scorpionates
Pellei, M., Papini, G., Lobbia, G. G., & Santini, C. (2009) · Current Bioactive Compounds · doi:10.2174/157340709789816456 · Cited by 18
He, S., Yang, H., Cao, R.-Q., Tang, Q., An, Y., & Wang, L. (2022) · Scientia Horticulturae · doi:10.1016/j.scienta.2022.111294 · Cited by 16
Benoit, S. L., & Maier, R. J. (2018) · Scientific Reports · doi:10.1038/s41598-018-32509-9 · Cited by 16
Breastfed Infants Metabolize Perchlorate
Shelor, C. P., Kirk, A. B., Dasgupta, P. Κ., Kroll, M., Campbell, C. A., & Choudhary, P. K. (2012) · Environmental Science & Technology · doi:10.1021/es2042806 · Cited by 15
Sulphate-reducing bacteria (SRB) and biocorrosion
Dall’Agnol, L. T., & Moura, J. J. G. (2014) · Elsevier eBooks · doi:10.1533/9781782421252.1.77 · Cited by 14
Self-citationNitrate–Nitrite Interplay in the Nitrogen Biocycle
Maiti, B. K., Moura, I., & Moura, J. J. G. (2025) · Molecules · doi:10.3390/molecules30143023 · Cited by 17
Self-citationLiu, M., Nazemi, A., Taylor, M. G., Nandy, A., Duan, C., Steeves, A. H., & Kulik, H. J. (2021) · ACS Catalysis · doi:10.1021/acscatal.1c04624 · Cited by 15
Tsai, C.-L., & Tainer, J. A. (2017) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.11.006 · Cited by 16
Coelho, C., Trincão, J., & Romão, M. J. (2009) · Journal of Crystal Growth · doi:10.1016/j.jcrysgro.2009.11.060 · Cited by 13
Self-citationModel Plants and Crop Improvement
Varshney, R. K., & Koebner, R. M. D. (2006) · CRC Press eBooks · doi:10.1201/9781420004618 · Cited by 13
Carmona, M. C., Amigó, M., Barceló-Batllori, S., Julià, M., Esteban, Y., Moreno, S., & Gomis, R. (2009) · International Journal of Obesity · doi:10.1038/ijo.2009.34 · Cited by 12
Design, synthesis, and characterization of a sterically encumbered dioxo molybdenum (VI) core
Sengar, R. S., & Basu, P. (2006) · Inorganica Chimica Acta · doi:10.1016/j.ica.2006.10.041 · Cited by 12
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