The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods
Open accessAbstract
Background The periplasmic nitrate reductase (NAP) from the sulphate reducing bacterium Desulfovibrio desulfuricans ATCC 27774 is induced by growth on nitrate and catalyses the reduction of nitrate to nitrite for respiration. NAP is a molybdenum-containing enzyme with one bis-molybdopterin guanine dinucleotide (MGD) cofactor and one [4Fe-4S] cluster in a single polypeptide chain of 723 amino acid residues. To date, there is no crystal structure of a nitrate reductase.Results The first crystal structure of a dissimilatory (respiratory) nitrate reductase was determined at 1.9 A resolution by multiwavelength anomalous diffraction (MAD) methods. The structure is folded into four domains with an alpha/beta-type topology and all four domains are involved in cofactor binding. The [4Fe-4S] centre is located near the periphery of the molecule, whereas the MGD cofactor extends across the interior of the molecule interacting with residues from all four domains. The molybdenum atom is located at the bottom of a 15 A deep crevice, and is positioned 12 A from the [4Fe-4S] cluster. The structure of NAP reveals the details of the catalytic molybdenum site, which is coordinated to two MGD cofactors, Cys140, and a water/hydroxo ligand. A facile electron-transfer pathway through bonds connects the molybdenum and the [4Fe-4S] cluster.Conclusions The polypeptide fold of NAP and the arrangement of the cofactors is related to that of Escherichia coli formate dehydrogenase (FDH) and distantly resembles dimethylsulphoxide reductase. The close structural homology of NAP and FDH shows how small changes in the vicinity of the molybdenum catalytic site are sufficient for the substrate specificity.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“In addition to four dithiolene sulfurs, a fifth sulfur ligand derived from a conserved cysteine residue coordinates the Mo in the active site of NapA.96,119,186”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [119]
Citations
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,394
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616
Solvent content of protein crystals
Matthews, B. W. (1968) · Journal of Molecular Biology · doi:10.1016/0022-2836(68)90205-2 · Cited by 7,970
LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
Wallace, A. C., Laskowski, R. A., & Thornton, J. M. (1995) · Protein Engineering Design and Selection · doi:10.1093/protein/8.2.127 · Cited by 5,731
Cell biology and molecular basis of denitrification
Zumft, W. G. (1997) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.61.4.533-616.1997 · Cited by 3,560
X-PLOR Version 3.1: A System for X-ray Crystallography and NMR
Brünger, A. T. (1992) · Medical Entomology and Zoology · Cited by 3,424
Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement
Engh, R., & Huber, R. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767391001071 · Cited by 2,497
Self-citation
Research works printed but not linked: 4
- Senez, 1958, Reduction of nitrite by molecular hydrogen by Desulfovibrio desulfuricans and other bacteria, Bull. Soc. Chim. Biol. Paris, 40, 2099
- Cowtan, 1994, ‘DM’: an automated procedure for phase improvement by density modification, Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography, 31, 34
- Hille, 1985, 7, 443
- Allen, 1993, 3D search and research using the Cambridge structural database, Chem. Des. Automation News, 8, 31
Cited by
Sorted by citations
The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738
Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers
Liu, J., Chakraborty, S., Hosseinzadeh, P., Yu, Y., Tian, S., Petrik, I. D., Bhagi, A., & Lu, Y. (2014) · Chemical Reviews · doi:10.1021/cr400479b · Cited by 905
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
Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus
Sazanov, L. A., & Hinchliffe, P. (2006) · Science · doi:10.1126/science.1123809 · Cited by 763
Arsenic and Selenium in Microbial Metabolism
Stolz, J. F., Basu, P., Santini, J. M., & Oremland, R. S. (2006) · Annual Review of Microbiology · doi:10.1146/annurev.micro.60.080805.142053 · Cited by 663
C-h⋯π-interactions in proteins
Brandl, M., Weiss, M. S., Jabs, A., Sühnel, J., & Hilgenfeld, R. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4473 · Cited by 649
Biology of Pseudomonas stutzeri
Lalucat, J., Bennasar-Figueras, A., Bosch, R., Garcı́a-Valdés, E., & Palleroni, N. J. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00047-05 · Cited by 639
Quantum Chemical Studies of Mechanisms for Metalloenzymes
Blomberg, M. R. A., Borowski, T., Himo, F., Liao, R., & Siegbahn, P. E. M. (2014) · Chemical Reviews · doi:10.1021/cr400388t · Cited by 606
Moreno‐Vivián, C., Cabello, P., Martínez‐Luque, M., Blasco, R., & del Castillo, F. J. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.21.6573-6584.1999 · Cited by 593
Richardson, D. J. (2000) · Microbiology · doi:10.1099/00221287-146-3-551 · Cited by 544
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
Synthetic Analogues and Reaction Systems Relevant to the Molybdenum and Tungsten Oxotransferases
Enemark, J. H., Cooney, J. J. A., Wang, J., & Holm, R. H. (2003) · Chemical Reviews · doi:10.1021/cr020609d · Cited by 475
Microbial nitrate respiration – Genes, enzymes and environmental distribution
Kraft, B., Strous, M., & Tegetmeyer, H. E. (2011) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2010.12.025 · Cited by 485
Dissimilatory Sulfate- and Sulfur-Reducing Prokaryotes
Rabus, R., Hansen, T. A., & Widdel, F. (2013) · Springer eBooks · doi:10.1007/978-3-642-30141-4_70 · Cited by 444
Chapter 2 Biochemistry, Physiology and Biotechnology of Sulfate‐Reducing Bacteria
Barton, L. L., & Fauque, G. D. (2009) · Advances in applied microbiology · doi:10.1016/s0065-2164(09)01202-7 · Cited by 461
Molybdenum and tungsten in biology
Hille, R. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02107-2 · Cited by 439
Nitrate and periplasmic nitrate reductases
Sparacino-Watkins, C., Stolz, J. F., & Basu, P. (2014) · Chem. Soc. Rev. · doi:10.1039/c3cs60249d · Cited by 426
Enzymology and bioenergetics of respiratory nitrite ammonification
Simon, J. (2002) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2002.tb00616.x · Cited by 403
Rabus, R., Venceslau, S. S., Wöhlbrand, L., Voordouw, G., Wall, J. D., & Pereira, I. A. C. (2015) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2015.05.002 · Cited by 366
Nitrate reduction and the nitrogen cycle in archaea
Cabello, P., Roldán, M. D., & Moreno‐Vivián, C. (2004) · Microbiology · doi:10.1099/mic.0.27303-0 · Cited by 337
Ellis, P. J., Conrads, T. P., Hille, R., & Kühn, P. (2001) · Structure · doi:10.1016/s0969-2126(01)00566-4 · Cited by 323
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-citationDissimilatory Sulfate- and Sulfur-Reducing Prokaryotes
Rabus, R., Hansen, T. A., & Widdel, F. (2006) · The Prokaryotes · doi:10.1007/0-387-30742-7_22 · Cited by 276
Inorganic nitrogen metabolism in bacteria
Richardson, D. J., & Watmough, N. J. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80034-9 · Cited by 264
A critical review of aerobic denitrification: Insights into the intracellular electron transfer
Yang, J., Feng, L. D., Pi, S., Cui, D., Ma, F., Zhao, H., & Li, A. (2020) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2020.139080 · Cited by 272
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
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
Zhou, D., Tong, Z., Song, Y., Han, Y., Pei, D., Pang, X., Zhai, J., Li, M., Cui, B., Qi, Z., et al. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.15.5147-5152.2004 · Cited by 208
Molybdoproteomes and Evolution of Molybdenum Utilization
Zhang, Y., & Gladyshev, V. N. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.03.051 · Cited by 198
Bacterial Adaptation of Respiration from Oxic to Microoxic and Anoxic Conditions: Redox Control
Bueno, E., Mesa, S., Bedmar, E. J., Richardson, D. J., & Delgado, M. J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4051 · Cited by 206
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-citationStructure and function of eukaryotic NAD(P)H:nitrate reductase
Campbell, W. H. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000847 · 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-citationShapleigh, J. P. (2006) · Springer eBooks · doi:10.1007/0-387-30742-7_23 · Cited by 177
Coevolution of metal availability and nitrogen assimilation in cyanobacteria and algae
GLASS, J. B., WOLFE‐SIMON, F., & ANBAR, A. D. (2009) · Geobiology · doi:10.1111/j.1472-4669.2009.00190.x · Cited by 174
Crystal Structure of Ethylbenzene Dehydrogenase from Aromatoleum aromaticum
Kloer, D. P., Hagel, C., Heider, J., & Schulz, G. E. (2006) · Structure · doi:10.1016/j.str.2006.07.001 · Cited by 176
The prokaryotic Mo/W-bisPGD enzymes family: A catalytic workhorse in bioenergetic
Grimaldi, S., Schoepp‐Cothenet, B., Ceccaldi, P., Guigliarelli, B., & Magalon, A. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.01.011 · Cited by 164
Genes involved in the anaerobic degradation of toluene in a denitrifying bacterium, strain EbN1
Kube, M., Heider, J., Amann, J., Hufnagel, P., Kühner, S., Beck, A., Reinhardt, R., & Rabus, R. (2004) · Archives of Microbiology · doi:10.1007/s00203-003-0627-3 · Cited by 158
Fischer, K., Barbier, G. G., Hecht, H. J., Mendel, R. R., Campbell, W. H., & Schwarz, G. (2005) · The Plant Cell · doi:10.1105/tpc.104.029694 · Cited by 160
Holm, R. H., Solomon, E. I., Majumdar, A., & Tenderholt, A. L. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.10.017 · Cited by 157
Alternative FeS cluster ligands: tuning redox potentials and chemistry
Bak, D. W., & Elliott, S. J. (2014) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2013.12.015 · Cited by 157
Nitrate reduction in the periplasm of gram-negative bacteria
Potter, L., Angove, H., Richardson, D., & Cole, J. (2001) · Advances in Microbial Physiology · doi:10.1016/s0065-2911(01)45002-8 · Cited by 152
Bioinorganic chemistry of molybdenum and tungsten enzymes: A structural–functional modeling approach
Majumdar, A., & Sarkar, S. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.11.027 · Cited by 152
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
Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase
Seiffert, G. B., Ullmann, G. M., Messerschmidt, A., Schink, B., Kroneck, P. M. H., & Einsle, O. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610407104 · Cited by 145
Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases
Moura, J. J. G., Brondino, C. D., Trinc�o, J., & Rom�o, M. J. (2004) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-004-0573-9 · Cited by 141
Self-citationEnzyme Mimetic Active Intermediates for Nitrate Reduction in Neutral Aqueous Media
Li, Y., Go, Y. K., Ooka, H., He, D., Jin, F., Kim, S. H., & Nakamura, R. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202002647 · Cited by 140
Schrader, N., Fischer, K., Theis, K. W., Mendel, R. R., Schwarz, G., & Kisker, C. (2003) · Structure · doi:10.1016/j.str.2003.09.001 · Cited by 141
The molybdenum oxotransferases and related enzymes
Hille, R. (2013) · Dalton Transactions · doi:10.1039/c2dt32376a · Cited by 133
Lim, B. S., Donahue, J. P., & Holm, R. H. (1999) · Inorganic Chemistry · doi:10.1021/ic9908672 · Cited by 134
McDevitt, C. A., Hugenholtz, P., Hanson, G. R., & McEwan, A. G. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02978.x · Cited by 123
Formate dehydrogenase – a versatile enzyme in changing environments
Jormakka, M., Byrne, B., & Iwata, S. (2003) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(03)00098-8 · Cited by 123
McEwan, A. G., Ridge, J. P., McDevitt, C. A., & Hugenholtz, P. (2002) · Geomicrobiology Journal · doi:10.1080/014904502317246138 · Cited by 123
Jepson, B. J. N., Mohan, S., Clarke, T. A., Gates, A. J., Cole, J. A., Butler, C. S., Butt, J. N., Hemmings, A. M., & Richardson, D. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607353200 · Cited by 120
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
Evidence of molybdenum association with particulate organic matter under sulfidic conditions
Dahl, T. W., Chappaz, A., Hoek, J., McKenzie, C. J., Svane, S., & Canfield, D. E. (2016) · Geobiology · doi:10.1111/gbi.12220 · Cited by 114
Respiratory arsenate reductase as a bidirectional enzyme
Richey, C. A., Chovanec, P., Hoeft, S. E., Oremland, R. S., Basu, P., & Stolz, J. F. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.03.045 · Cited by 111
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-citationStructural and Biochemical Identification of a Novel Bacterial Oxidoreductase
Loschi, L., Brokx, S. J., Hills, T. L., Zhang, G., Bertero, M. G., Lovering, A. L., Weiner, J. H., & Strynadka, N. C. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408876200 · Cited by 108
Nitrate reductases: Structure, functions, and effect of stress factors
Morozkina, E. V., & Zvyagilskaya, R. A. (2007) · Biochemistry (Moscow) · doi:10.1134/s0006297907100124 · Cited by 103
Structural basis of denitrification
Einsle, O., & Kroneck, P. M. H. (2004) · Biological Chemistry · doi:10.1515/bc.2004.115 · Cited by 97
Flanagan, D., Gregory, L. G., Carter, J. P., Karakas-Sen, A., Richardson, D. J., & Spiro, S. (1999) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1999.tb13742.x · Cited by 97
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-citationStructural and mechanistic insights on nitrate reductases
Coelho, C., & Romão, M. J. (2015) · Protein Science · doi:10.1002/pro.2801 · Cited by 98
Self-citationStructural aspects of denitrifying enzymes
Moura, I., & Moura, J. J. G. (2001) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00187-3 · Cited by 96
Self-citationBiomimetic Chemistry of Iron, Nickel, Molybdenum, and Tungsten in Sulfur-Ligated Protein Sites
Groysman, S., & Holm, R. H. (2009) · Biochemistry · doi:10.1021/bi900044e · Cited by 98
POTTER, L. C., & COLE, J. A. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3440069 · Cited by 93
Protonmotive force generation by a redox loop mechanism
Jormakka, M., Byrne, B., & Iwata, S. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00389-2 · Cited by 91
Elliott, S. J., Hoke, K. R., Heffron, K., Palak, M., Rothery, R. A., Weiner, J. H., & Armstrong, F. A. (2004) · Biochemistry · doi:10.1021/bi035869j · Cited by 90
Spectroscopic studies of molybdenum and tungsten enzymes
Pushie, M. J., & George, G. N. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.01.056 · Cited by 86
Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases
Maia, L. B., & Moura, J. J. G. (2015) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-014-1234-2 · Cited by 88
Self-citationEnzyme Electrochemistry — Biocatalysis on an Electrode
Bernhardt, P. V. (2006) · Australian Journal of Chemistry · doi:10.1071/ch05340 · Cited by 83
Rothery, R. A., Bertero, M. G., Cammack, R., Palak, M., Blasco, F., Strynadka, N. C. J., & Weiner, J. H. (2004) · Biochemistry · doi:10.1021/bi049938l · Cited by 81
Simon, J., Sänger, M., Schuster, S. C., & Groß, R. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03544.x · Cited by 81
Tuning a Nitrate Reductase for Function
Jepson, B. J. N., Anderson, L. J., Rubio, L. M., Taylor, C. J., Butler, C. S., Flores, E., Herrero, A., Butt, J. N., & Richardson, D. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402669200 · Cited by 79
Simpson, P. J. L., Richardson, D. J., & Codd, R. (2009) · Microbiology · doi:10.1099/mic.0.034421-0 · Cited by 79
Pan, Y. C., Xu, H., Zhu, H., Huang, C., Zhang, Z., & Li, G. (2025) · Journal of Materials Chemistry A · doi:10.1039/d5ta02848e · Cited by 77
The Trigonal Prism in Coordination Chemistry
Cremades, E., Echeverría, J., & Álvarez, S. (2010) · Chemistry - A European Journal · doi:10.1002/chem.200903032 · Cited by 74
Leopoldini, M., Russo, N., Toscano, M., Dułak, M., & Wesołowski, T. A. (2006) · Chemistry - A European Journal · doi:10.1002/chem.200500790 · Cited by 76
Structural aspects of mononuclear Mo/W-enzymes
Dobbek, H. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.11.017 · Cited by 78
Protein Network of the Pseudomonas aeruginosa Denitrification Apparatus
Acuña, J. M. B., Rohde, M., Wissing, J. B., Jänsch, L., Schobert, M., Molinari, G., Timmis, K. N., Jahn, M., & Jahn, D. (2016) · Journal of Bacteriology · doi:10.1128/jb.00055-16 · Cited by 74
ModE-Dependent Molybdate Regulation of the Molybdenum Cofactor OperonmoainEscherichia coli
Anderson, L. A., McNairn, E., Leubke, T., Pau, R. N., & Boxer, D. H. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.24.7035-7043.2000 · Cited by 71
Thapper, A., Deeth, R. J., & Nordlander, E. (2002) · Inorganic Chemistry · doi:10.1021/ic020385h · Cited by 70
Lake, M. W., Temple, C. A., Rajagopalan, K. V., & Schindelin, H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007406200 · Cited by 72
Marietou, A., Richardson, D., Cole, J., & Mohan, S. (2005) · FEMS Microbiology Letters · doi:10.1016/j.femsle.2005.05.042 · Cited by 68
Quan, D., Shim, J. H., Kim, J.-D., Park, H. S., Cha, G. S., & Nam, H. (2005) · Analytical Chemistry · doi:10.1021/ac050198b · Cited by 68
Rebelo, J., Macieira, S., Dias, J. M. L., Huber, R., Ascenso, C. S., Rusnak, F. M., Moura, J. J. G., Moura, I., & Romão, M. J. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3552 · Cited by 67
Self-citationNADH dehydrogenases: from basic science to biomedicine
Yagi, T., Seo, B. B., Bernardo, S. D., Nakamaru-Ogiso, E., Kao, M.-C., & Matsuno-Yagi, A. (2001) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1010787004053 · Cited by 63
Fu, W., Song, G., Wang, Y., Wang, Q., Duan, P., Liu, C., Zhang, X., & Rao, Z. (2022) · Frontiers in Environmental Science · doi:10.3389/fenvs.2022.887093 · Cited by 63
Nakamaru‐Ogiso, E., Yano, T., Yagi, T., & Ohnishi, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410377200 · Cited by 62
Temple, C. A., & Rajagopalan, K. V. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007407200 · Cited by 62
Ab Inito Modeling of Ethylbenzene Dehydrogenase Reaction Mechanism
Szaleniec, M., Borowski, T., Schühle, K., Witko, M., & Heider, J. (2010) · Journal of the American Chemical Society · doi:10.1021/ja907208k · Cited by 62
Nitrate biosensors and biological methods for nitrate determination
Sohail, M., & Adeloju, S. B. O. (2016) · Talanta · doi:10.1016/j.talanta.2016.03.002 · Cited by 61
Molybdopterin from molybdenum and tungsten enzymes
Schindelin, H., Kisker, C., & Rajagopalan, K. V. (2001) · Advances in protein chemistry · doi:10.1016/s0065-3233(01)58002-x · Cited by 58
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-citationDenitrification in foraminifera has an ancient origin and is complemented by associated bacteria
Woehle, C., Roy, A.-S., Glock, N., Michels, J., Wein, T., Weißenbach, J., Romero, D., Hiebenthal, C., Gorb, S. N., Schönfeld, J., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2200198119 · Cited by 57
Rapid detection of nutrients with electronic sensors: a review
Chen, X.-Y., Zhou, G., Mao, S., & Chen, J. (2018) · Environmental Science Nano · doi:10.1039/c7en01160a · 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-citation
Metadata
- Authors
- Dias, J. M., Than, M. E., Humm, A., Huber, R., Bourenkov, G. P., Bartunik, H. D., Bursakov, S., Calvete, J., Caldeira, J., Carneiro, C., Moura, J. J., Moura, I., & Romão, M. J.
- Affiliations
- Universidade Nova de Lisboa (PT)
- Max Planck Institute of Biochemistry (DE)
- Deutsches Elektronen-Synchrotron DESY (DE)
- A N Bach Institute of Biochemistry (RU)
- Corresponding author
- Romão, Maria J
- ORCID
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 1999-01
- Volume
- 7
- Issue
- 1
- Pages
- 65-79
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W2086606027
- Cited by
- 286
- References
- 68
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 5 · 2023: 2 · 2022: 7 · 2021: 5 · 2020: 8 · 2019: 5 · 2018: 5 · 2017: 3 · 2016: 8 · 2015: 7 · 2014: 12 · 2013: 13 · 2012: 5
- FWCI
- 22.39
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Structure (publishedVersion)
- PubMed (publishedVersion)
- Desy Publications Database (Deutsches Elektronen-Synchrotron DESY) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- periplasmic nitrate reductase, Desulfovibrio desulfuricans, dissimilatory nitrate reduction, molybdenum enzymes, [4Fe-4S] cluster, cofactor binding, electron transfer pathway, substrate specificity
- MeSH terms
- Amino Acid Sequence, Cloning, Molecular, Desulfovibrio, Guanine Nucleotides, Iron-Sulfur Proteins, Models, Molecular, Molecular Sequence Data, Molybdenum, Nitrate Reductases, Organometallic Compounds, Protein Conformation, Recombinant Proteins, X-Ray Diffraction, Polymerase Chain Reaction, Sequence Alignment, Sequence Homology, Amino Acid, Protein Structure, Secondary, Crystallography, X-Ray, 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