Models for Molybdenum Coordination during the Catalytic Cycle of Periplasmic Nitrate Reductase from Paracoccus denitrificans Derived from EPR and EXAFS Spectroscopy

Colorimetric Methods of Analyses

Snell, F. D., & Snell, C. T. (1950) · Soil Science · doi:10.1097/00010694-195002000-00009 · Cited by 1,415 · see citing works

Sites and specificity of the reaction of bipyridylium compounds with anaerobic respiratory enzymes of Escherichia coli. Effects of permeability barriers imposed by the cytoplasmic membrane

Jones, R. W., & Garland, P. B. (1977) · Biochemical Journal · doi:10.1042/bj1640199 · Cited by 268 · see citing works

Crystal 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 · see citing works

Transfer of Thiosphaera pantotropha to Paracoccus denitrificans

Ludwig, W., Mittenhuber, G., & Friedrich, C. G. (1993) · International Journal of Systematic Bacteriology · doi:10.1099/00207713-43-2-363 · Cited by 185 · see citing works

Crystal structure of oxidized trimethylamine N -oxide reductase from Shewanella massilia at 2.5 å resolution 1 1Edited by R. Huber

Czjzek, M., Santos, J. D., Pommier, J., Giordano, G., Méjean, V., & Haser, R. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2156 · Cited by 173 · see citing works

Molybdenum active centre of DMSO reductase from Rhodobacter capsulatus: crystal structure of the oxidised enzyme at 1.82-Å resolution and the dithionite-reduced enzyme at 2.8-Å resolution

McAlpine, A. S., McEwan, A. G., Shaw, A. L., & Bailey, S. (1997) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050185 · Cited by 145 · see citing works

The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha

Berks, B. C., Richardson, D. J., Reilly, A., Willis, A. C., & Ferguson, S. J. (1995) · Biochemical Journal · doi:10.1042/bj3090983 · Cited by 138 · see citing works

The respiratory nitrate reductase from Paracoccus denitrificans. Molecular characterisation and kinetic properties

CRASKE, A. L., & Ferguson, S. J. (1986) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1986.tb09771.x · Cited by 131 · see citing works

Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha

Berks, B. C., RICHARDSON, D. J., Robinson, C. V., Reilly, A., Aplin, R. T., & Ferguson, S. J. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb18605.x · Cited by 115 · see citing works

Molybdenum(VI) and molybdenum(V) complexes with N,N'-dimethyl-N,N'-bis(2-mercaptophenyl)ethylenediamine. Electrochemical and electron paramagnetic resonance models for the molybdenum(VI/V) centers of the molybdenum hydroxylases and related enzymes

Dowerah, D., Spence, J. T., Singh, R., Wedd, A. G., Wilson, G. L., Farchione, F., Enemark, J. H., Kristofzski, J. G., & Bruck, M. A. (1987) · Journal of the American Chemical Society · doi:10.1021/ja00253a016 · Cited by 108 · see citing works

Multiple States of the Molybdenum Centre of Dimethylsulphoxide Reductase from Rhodobacter Capsulatus Revealed by EPR Spectroscopy

Bennett, B., Benson, N., McEwan, A. G., & Bray, R. C. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.00321.x · Cited by 86 · see citing works

Complexes with halide and other anions of the molybdenum centre of nitrate reductase from Escherichia coli

George, G. N., Bray, R. C., Morpeth, F. F., & Boxer, D. H. (1985) · Biochemical Journal · doi:10.1042/bj2270925 · Cited by 63 · see citing works

Characterization of the paramagnetic iron‐containing redox centres of Thiosphaera pantotropha periplasmic nitrate reductase

BRETON, J. L., Berks, B. C., Reilly, A., THOMSON, A. J., Ferguson, S. J., & Richardson, D. J. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00445-5 · Cited by 59 · see citing works

Mo(V) Electron Paramagnetic Resonance Signals from the Periplasmic Nitrate Reductase of <i>Thiosphaera Pantotropha</i>

Bennett, B., Berks, B. C., Ferguson, S. J., Thomson, A. J., & Richardson, D. J. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.00789.x · Cited by 58 · see citing works

X-ray absorption spectroscopy of dimethylsulfoxide reductase from Rhodobacter capsulatus

Baugh, P. E., Garner, C. D., Charnock, J., Collison, D., Davies, E. S., McAlpine, A. S., Bailey, S., Lane, I. C., Hanson, G. R., & McEwan, A. G. (1997) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050178 · Cited by 55 · see citing works

Purification and characterization of the assimilatory nitrate reductase of Azotobacter vinelandii

Gangeswaran, R., Lowe, D., & Eady, R. R. (1993) · Biochemical Journal · doi:10.1042/bj2890335 · Cited by 55 · see citing works

Identification of an assimilatory nitrate reductase in mutants of Paracoccus denitrificans GB17 deficient in nitrate respiration

Sears, H. J., Little, P. J., Richardson, D. J., Berks, B. C., Spiro, S., & Ferguson, S. J. (1997) · Archives of Microbiology · doi:10.1007/s002030050417 · Cited by 31 · see citing works

Structural investigation of the molybdenum site of the periplasmic nitrate reductase from Thiosphaera pantotropha by X-ray absorption spectroscopy

Bennett, B., Charnock, J., Sears, H. J., Berks, B. C., THOMSON, A. J., Ferguson, S. J., Garner, C. D., & RICHARDSON, D. J. (1996) · Biochemical Journal · doi:10.1042/bj3170557 · Cited by 20 · see citing works

31st Rocky Mountain Conference

(1989) · doi:10.56902/rmcmr.1989.31.1 · Cited by 8 · see citing works

The mononuclear molybdenum enzymes

Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738 · see citing works

Bacterial respiration: a flexible process for a changing environment 1999 Fleming Lecture (Delivered at the 144th meeting of the Society for General Microbiology, 8 September 1999)

Richardson, D. J. (2000) · Microbiology · doi:10.1099/00221287-146-3-551 · Cited by 544 · see citing works

Functional, biochemical and genetic diversity of prokaryotic nitrate reductases

Richardson, D. J., Berks, B. C., Russell, D. A., Spiro, S., & Taylor, C. J. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000845 · Cited by 466 · see citing works

Nitrate and periplasmic nitrate reductases

Sparacino-Watkins, C., Stolz, J. F., & Basu, P. (2014) · Chem. Soc. Rev. · doi:10.1039/c3cs60249d · Cited by 426 · see citing works

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 273 · see citing works

Metalloenzymes of the denitrification pathway

Tavares, P., Pereira, A. S., Moura, J. J. G., & Moura, I. (2006) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2006.09.003 · Cited by 228 · see citing works

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Jormakka, M., Richardson, D. J., Byrne, B., & Iwata, S. (2004) · Structure · doi:10.1016/j.str.2003.11.020 · Cited by 212 · see citing works

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Zheng, X., Su, Y., Chen, Y., Wan, R., Liu, K., Li, M., & Yin, D. (2014) · Environmental Science & Technology · doi:10.1021/es504251v · Cited by 185 · see citing works

Molybdenum and tungsten enzymes: a crystallographic and mechanistic overview

Romão, M. J. (2009) · Dalton Transactions · doi:10.1039/b821108f · Cited by 182 · see citing works

Sulfite:Cytochrome c Oxidoreductase fromThiobacillus novellus

Kappler, U., Bennett, B., Rethmeier, J., Schwarz, G., Deutzmann, R., McEwan, A. G., & Dahl, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.18.13202 · Cited by 175 · see citing works

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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 159 · see citing works

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Potter, L., Angove, H., Richardson, D., & Cole, J. (2001) · Advances in Microbial Physiology · doi:10.1016/s0065-2911(01)45002-8 · Cited by 152 · see citing works

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Stewart, V. J., Lu, Y., & Darwin, A. J. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.5.1314-1323.2002 · Cited by 144 · see citing works

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 · see citing works

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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 · see citing works

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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 · see citing works

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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 · see citing works

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Martínez‐Espinosa, R. M., Dridge, E. J., Bonete, M.-J., Butt, J. N., Butler, C. S., Sargent, F., & Richardson, D. J. (2007) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2007.00887.x · Cited by 110 · see citing works

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Morozkina, E. V., & Zvyagilskaya, R. A. (2007) · Biochemistry (Moscow) · doi:10.1134/s0006297907100124 · Cited by 103 · see citing works

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Ridley, H., Watts, C. A., Richardson, D. J., & Butler, C. S. (2006) · Applied and Environmental Microbiology · doi:10.1128/aem.00568-06 · Cited by 96 · see citing works

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Meakin, G. E., Bueno, E., Jepson, B. J. N., Bedmar, E. J., Richardson, D. J., & Delgado, M. J. (2007) · Microbiology · doi:10.1099/mic.0.2006/000059-0 · Cited by 96 · see citing works

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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 · see citing works

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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 · see citing works

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Pushie, M. J., & George, G. N. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.01.056 · Cited by 86 · see citing works

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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 · see citing works

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Lim, B. S., Willer, M. W., Miao, M.-M., & Holm, R. H. (2001) · Journal of the American Chemical Society · doi:10.1021/ja010786g · Cited by 78 · see citing works

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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 62 · see citing works

Characterization of the Iron-Sulfur Cluster N7 (N1c) in the Subunit NuoG of the Proton-translocating NADH-quinone Oxidoreductase from Escherichia coli

Nakamaru‐Ogiso, E., Yano, T., Yagi, T., & Ohnishi, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410377200 · Cited by 62 · see citing works

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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 · see citing works

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Jepson, B. J. N., Marietou, A., Mohan, S. B., Cole, J. A., Butler, C. S., & Richardson, D. J. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340122 · Cited by 54 · see citing works

Properties of the periplasmic nitrate reductases from<i>Paracoccus pantotrophus</i>and<i>Escherichia coli</i>after growth in tungsten-supplemented media

Gates, A. J., Hughes, R. O., Sharp, S. R., Millington, P. D., Nilavongse, A., Cole, J. A., Leach, E.-R., Jepson, B., Richardson, D. J., & Butler, C. S. (2003) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(03)00122-8 · Cited by 53 · see citing works

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Fourmond, V., Burlat, B., Dementin, S., Arnoux, P., Sabaty, M., Boiry, S., Guigliarelli, B., Bertrand, P., Pignol, D., & Léger, C. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp807092y · Cited by 51 · see citing works

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Cole, J. A., & Richardson, D. J. (2008) · EcoSal Plus · doi:10.1128/ecosal.3.2.5 · Cited by 48 · see citing works

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Wang, D. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00427 · Cited by 46 · see citing works

EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774

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 · see citing works

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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 · see citing works

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van Spanning, R. J. M., Delgado, M. J., & Richardson, D. J. (2005) · Springer eBooks · doi:10.1007/1-4020-3544-6_13 · Cited by 44 · see citing works

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González, 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 44 · see citing works

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Gates, A. J., Richardson, D. J., & Butt, J. N. (2007) · Biochemical Journal · doi:10.1042/bj20071088 · Cited by 43 · see citing works

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Biaso, F., Burlat, B., & Guigliarelli, B. (2012) · Inorganic Chemistry · doi:10.1021/ic201533p · Cited by 40 · see citing works

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Su, X., Chen, Y., Wang, Y., Yang, X., & He, Q. (2019) · Soil Biology and Biochemistry · doi:10.1016/j.soilbio.2019.03.024 · Cited by 38 · see citing works

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Prange, A., & Modrow, H. (2002) · Reviews in Environmental Science and Bio/Technology · doi:10.1023/a:1023281303220 · Cited by 36 · see citing works

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Jacques, J. G. J., Fourmond, V., Arnoux, P., Sabaty, M., Étienne, É., Grosse, S., Biaso, F., Bertrand, P., Pignol, D., Léger, C., et al. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.10.013 · Cited by 35 · see citing works

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Watts, C. A., Ridley, H., Dridge, E. J., Leaver, J. T., Reilly, A. J., Richardson, D. J., & Butler, C. S. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330173 · Cited by 35 · see citing works

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Gates, A. J., Kemp, G. L., To, C. Y., Mann, J., Marritt, S. J., Mayes, A. G., Richardson, D. J., & Butt, J. N. (2011) · Physical Chemistry Chemical Physics · doi:10.1039/c0cp02887h · Cited by 33 · see citing works

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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 · see citing works

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Majumdar, A., Pal, K., & Sarkar, S. (2008) · Inorganic Chemistry · doi:10.1021/ic7024268 · Cited by 33 · see citing works

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Prisner, T. F., Lyubenova, S., Atabay, Y., MacMillan, F., Kröger, A., & Klimmek, O. (2003) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-002-0432-5 · Cited by 33 · see citing works

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BUTLER, C. S., CHARNOCK, J. M., GARNER, C. D., THOMSON, A. J., FERGUSON, S. J., BERKS, B. C., & RICHARDSON, D. J. (2000) · Biochemical Journal · doi:10.1042/bj3520859 · Cited by 32 · see citing works

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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 32 · see citing works

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Drew, S. C., Hill, J. P., Lane, I. C., Hanson, G. R., Gable, R. W., & Young, C. G. (2007) · Inorganic Chemistry · doi:10.1021/ic060585j · Cited by 31 · see citing works

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Mintmier, B., McGarry, J. M., Sparacino-Watkins, C. E., Sallmen, J. W., Fischer-Schrader, K., Magalon, A., McCormick, J. R., Stolz, J. F., Schwarz, G., Bain, D. J., et al. (2018) · FEMS Microbiology Letters · doi:10.1093/femsle/fny151 · Cited by 30 · see citing works

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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 · see citing works

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Kirk, M. L., & Stein, B. W. (2013) · Elsevier eBooks · doi:10.1016/b978-0-08-097774-4.00316-8 · Cited by 23 · see citing works

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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 · see citing works

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Arias-Cartín, R., Uzel, A., Seduk, F., Gerbaud, G., Pierrel, F., Broc, M., Lebrun, R., Guigliarelli, B., Magalon, A., Grimaldi, S., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101384 · Cited by 19 · see citing works

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Pellei, M., Papini, G., Lobbia, G. G., & Santini, C. (2009) · Current Bioactive Compounds · doi:10.2174/157340709789816456 · Cited by 17 · see citing works

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Wang, Y., & Zhang, B. (2020) · Journal of Energy Chemistry · doi:10.1016/j.jechem.2020.05.017 · Cited by 17 · see citing works

Isolation and spectroscopic characterization of the membrane-bound nitrate reductase from Pseudomonas chlororaphis DSM 50135

Pinho, D., Besson, S., Silva, P. J., de Castro, B., & Moura, I. (2005) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2005.02.008 · Cited by 17 · see citing works

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Butler, C. S., & Richardson, D. J. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330113 · Cited by 16 · see citing works

Enzyme 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 · doi:10.1002/ange.202002647 · Cited by 15 · see citing works

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Wang, Y., Wu, M., Lai, C.-Y., Lu, X., & Guo, J. (2023) · Environmental Science & Technology · doi:10.1021/acs.est.3c04958 · Cited by 13 · see citing works

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Butler, C. S., Ferguson, S. J., Berks, B. C., THOMSON, A. J., Cheesman, M. R., & Richardson, D. J. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02577-7 · Cited by 13 · see citing works

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Wang, T.-H., Chen, Y.-H., Huang, J.-Y., Liu, K., Ke, S., & Chu, H. (2011) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2011.07.007 · Cited by 13 · see citing works

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Clark, I. C., Melnyk, R. A., Youngblut, M. D., Carlson, H. K., Iavarone, A. T., & Coates, J. D. (2015) · mBio · doi:10.1128/mbio.00282-15 · Cited by 12 · see citing works

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Romão, M. J., Dias, J. M. L., & Moura, I. (2004) · Wiley eBooks · doi:10.1002/0470028637.met178 · Cited by 12 · see citing works

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Maia, L. B., Moura, I., & Moura, J. J. G. (2017) · Biological magnetic resonance · doi:10.1007/978-3-319-59100-1_4 · Cited by 10 · see citing works

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Gates, A. J., Butler, C. S., Richardson, D. J., & Butt, J. N. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390236 · Cited by 10 · see citing works

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Giri, N. C., Mintmier, B., Radhakrishnan, M., Mielke, J. W., Wilcoxen, J., & Basu, P. (2024) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-024-02057-x · Cited by 7 · see citing works

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Ridley, H., Watts, C. A., Richardson, D. J., & Butler, C. S. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2006.08.028 · Cited by 7 · see citing works

Isolated molybdenum-based microporous POMs for selective adsorption of gases

Deng, L. Q., Lin, R.-Y., & Zhou, Z. (2022) · Dalton Transactions · doi:10.1039/d2dt00134a · Cited by 6 · see citing works

Kinetic Studies of a Ferredoxin-Dependent Cyanobacterial Nitrate Reductase

Srivastava, A. P., Knaff, D. B., & Setif, P. Q. Y. (2014) · Biochemistry · doi:10.1021/bi500386n · Cited by 6 · see citing works

ESEEM and Mims ENDOR Spectroscopies of cis,trans-(L-N2S2)MoVO(SCH2Ph): Detection of the Two Benzylthiolate α Protons

Astashkin, A. V., Cosper, M. M., Raitsimring, A. M., & Enemark, J. H. (2000) · Inorganic Chemistry · doi:10.1021/ic000405k · Cited by 6 · see citing works

The Inhibition of Engineered Nano-ZnO in the Biological Nitrogen Removal Process: A Review

Ma, T., Hong-xi, M., Wu, J. H., Yu, Y., Chen, T., Yao, Y., Liao, W., & Feng, L. (2023) · Water · doi:10.3390/w16010017 · Cited by 4 · see citing works

Life on oxidised nitrogen: the biochemistry and physiology of prokaryotic life supported by the nitrate-nitrite redox couple

Richardson, D. J. (2025) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2025.07.004 · Cited by 3 · see citing works

Crown ether-like octanuclear molybdenum( v ) clusters for cation binding and gas adsorption

Dai, R.-D., Xie, Z., Liu, C., Dong, X. Y. M., & Zhou, Z. (2024) · Dalton Transactions · doi:10.1039/d4dt00825a · Cited by 3 · see citing works

The Metabolism of Nitrogen and Amino Acids

Metzler, D. E., Metzler, C. M., & Sauke, D. J. (2001) · Elsevier eBooks · doi:10.1016/b978-012492543-4/50027-1 · Cited by 3 · see citing works

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Mongkonpruthangkoon, C., Giri, N. C., & Basu, P. (2026) · Biochemical Society Transactions · doi:10.1042/bst20250033 · Cited by 2 · see citing works

Application of EPR and related methods to molybdenum-containing enzymes

Hille, R., & Niks, D. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.02.006 · Cited by 2 · see citing works

Chiral Supramolecular Microporous Thio-Oxomolybdenum(V) Tartrates for the Selective Adsorptions of Gases

Deng, L. Q., & Zhou, Z. (2022) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.2c02283 · Cited by 2 · see citing works

Binuclear, tetranuclear and hexadecanuclear thio-oxomolybdenum( v / iv ) glycolates with selective adsorptions of gases

Lin, R.-Y., Deng, L. Q., An, D., & Zhou, Z. (2022) · Dalton Transactions · doi:10.1039/d2dt03324k · Cited by 2 · see citing works

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Yang, J., Bae, M., Khadanand, K. C., Dong, X., Nguyen, Q. D., Mengell, J., Balskus, E. P., & Kirk, M. L. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c20654 · Cited by 1 · see citing works

Hexnuclear, octanuclear, dodecanuclear, and hexadecnuclear polyoxomolybdenum( v )-based porous materials for selective adsorption of gases

Lin, R.-Y., Dai, R.-D., Dong, X. Y. M., & Zhou, Z. (2023) · CrystEngComm · doi:10.1039/d3ce00736g · Cited by 1 · see citing works

Dissimilatory Nitrate Reductase

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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)

Periplasmic Nitrate Reduction

Cole, J. A. (2014) · ASM Press eBooks · doi:10.1128/9781555815806.ch14

Expression, purification and biochemical characterization of the periplasmic nitrate reductase NapA from Magnetospirillum gryphiswaldense MSR-1

Xu, C., Wan, H., Zhang, Y., Zhang, J., Chen, W., Li, M., Wang, J., Ma, K., Wang, Y., & Wang, J. (2026) · Protein Expression and Purification · doi:10.1016/j.pep.2026.106906

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Jacques, J. G. J. (2014) · theses.fr (ABES) · doi:10.70675/19852afbz7969z49e5z86b0z4baa30aa72b7

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Biaso, F., Burlat, B., & Guigliarelli, B. (2012) · Inorganic Chemistry · doi:10.1021/ic201533p · Cited by 40 · see citing works

Identification of periplasmic nitrate reductase Mo(V) EPR signals in intact cells of Paracoccus denitrificans

Sears, H. J., Bennett, B., Spiro, S., THOMSON, A. J., & Richardson, D. J. (1995) · Biochemical Journal · doi:10.1042/bj3100311 · Cited by 21 · see citing works

Mo(V) Electron Paramagnetic Resonance Signals from the Periplasmic Nitrate Reductase of <i>Thiosphaera Pantotropha</i>

Bennett, B., Berks, B. C., Ferguson, S. J., Thomson, A. J., & Richardson, D. J. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.00789.x · Cited by 58 · see citing works

Structural investigation of the molybdenum site of the periplasmic nitrate reductase from Thiosphaera pantotropha by X-ray absorption spectroscopy

Bennett, B., Charnock, J., Sears, H. J., Berks, B. C., THOMSON, A. J., Ferguson, S. J., Garner, C. D., & RICHARDSON, D. J. (1996) · Biochemical Journal · doi:10.1042/bj3170557 · Cited by 20 · see citing works

ORIGINAL PAPER

González, P. J., Rivas, G., Brondino, C. D., Sergey, Æ., Bursakov, A., Moura, I., Jose, Æ., & Moura, J. G. (2016)