The molybdenum oxotransferases and related enzymes

The mononuclear molybdenum enzymes

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

The Mononuclear Molybdenum Enzymes

Hille, R. (1996) · Chemical Reviews · doi:10.1021/cr950061t · Cited by 1,501 · see citing works

Molybdenum cofactors, enzymes and pathways

Schwarz, G., Mendel, R. R., & Ribbe, M. W. (2009) · Nature · doi:10.1038/nature08302 · Cited by 872 · see citing works

Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion

Enroth, C., Eger, B. T., Okamoto, K., Nishino, T., Nishino, T., & Pai, E. F. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.20.10723 · Cited by 733 · see citing works

Crystal Structure of Formate Dehydrogenase H: Catalysis Involving Mo, Molybdopterin, Selenocysteine, and an Fe 4 S 4 Cluster

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 · see citing works

The Arabidopsis LOS5/ABA3 Locus Encodes a Molybdenum Cofactor Sulfurase and Modulates Cold Stress- and Osmotic Stress-Responsive Gene Expression

Xiong, L., Ishitani, M., Lee, H., & Zhu, J. (2001) · The Plant Cell · doi:10.1105/tpc.010101 · Cited by 576 · see citing works

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 · see citing works

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 · see citing works

Molecular Basis of Sulfite Oxidase Deficiency from the Structure of Sulfite Oxidase

Kisker, C., Schindelin, H., Pacheco, A. A., Wehbi, W. A., Garrett, R. M., Rajagopalan, K. V., Enemark, J. H., & Rees, D. C. (1997) · Cell · doi:10.1016/s0092-8674(00)80488-2 · Cited by 485 · see citing works

Crystal Structure of the Xanthine Oxidase-Related Aldehyde Oxido-Reductase from D. gigas

Romão, M. J., Archer, M., Moura, I., Moura, J. J. G., LeGall, J., Engh, R. A., Schneider, M., Hof, P., & Huber, R. (1995) · Science · doi:10.1126/science.270.5239.1170 · Cited by 480 · 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

The Arabidopsis LOS5/ABA3 Locus Encodes a Molybdenum Cofactor Sulfurase and Modulates Cold Stress- and Osmotic Stress-Responsive Gene Expression

Xiong, L. (2001) · The Plant Cell · doi:10.1105/tpc.13.9.2063 · Cited by 455 · see citing works

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 451 · see citing works

Xanthine oxidase and xanthine dehydrogenase

Hille, R., & Nishino, T. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.11.7649415 · Cited by 445 · see citing works

Molybdenum and tungsten in biology

Hille, R. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02107-2 · Cited by 430 · see citing works

Catalysis at a dinuclear [CuSMo(O)OH] cluster in a CO dehydrogenase resolved at 1.1-Å resolution

Dobbek, H., Gremer, L., Kiefersauer, R. A., Huber, R., & Meyer, O. O. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212640899 · Cited by 387 · see citing works

Microbial metalloproteomes are largely uncharacterized

Cvetkovic, A., Menon, A. L., Thorgersen, M. P., Scott, J. W., Poole, F. L., Jenney, F. E., Lancaster, W. A., Praissman, J. L., Shanmukh, S., Vaccaro, B. J., et al. (2010) · Nature · doi:10.1038/nature09265 · Cited by 363 · see citing works

MOLYBDENUM COFACTOR BIOSYNTHESIS AND MOLYBDENUM ENZYMES

Schwarz, G., & Mendel, R. R. (2006) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.57.032905.105437 · Cited by 347 · see citing works

ABA3 Is a Molybdenum Cofactor Sulfurase Required for Activation of Aldehyde Oxidase and Xanthine Dehydrogenase in Arabidopsis thaliana

Bittner, F., Oreb, M., & Mendel, R. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100472200 · Cited by 332 · see citing works

Crystal Structure of the 100 kDa Arsenite Oxidase from Alcaligenes faecalis in Two Crystal Forms at 1.64 Å and 2.03 Å

Ellis, P. J., Conrads, T. P., Hille, R., & Kühn, P. (2001) · Structure · doi:10.1016/s0969-2126(01)00566-4 · Cited by 316 · see citing works

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 · see citing works

Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S -selanylcysteine

Dobbek, H., Gremer, L., Meyer, O. O., & Huber, R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.8884 · Cited by 255 · 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

A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes

Huber, R., Hof, P., Duarte, R. O., Moura, J. J., Moura, I., Liu, M. Y., LeGall, J., Hille, R., Archer, M., & Romão, M. J. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.17.8846 · Cited by 242 · see citing works

Molybdenum enzymes in higher organisms

Hille, R., Nishino, T., & Bittner, F. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.11.034 · Cited by 242 · see citing works

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 212 · see citing works

Crystal Structures of the Active and Alloxanthine-Inhibited Forms of Xanthine Dehydrogenase from Rhodobacter capsulatus

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 204 · see citing works

Identification and Biochemical Characterization ofArabidopsis thaliana Sulfite Oxidase

Eilers, T., Schwarz, G., Brinkmann, H., Witt, C., Richter, T., Nieder, J., Koch, B., Hille, R., Hänsch, R., & Mendel, R. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108078200 · Cited by 191 · see citing works

Identification of the Missing Component in the Mitochondrial Benzamidoxime Prodrug-converting System as a Novel Molybdenum Enzyme

Havemeyer, A., Bittner, F., Wollers, S., Mendel, R. R., Kunze, T., & Clement, B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607697200 · Cited by 186 · see citing works

Structure and function of eukaryotic NAD(P)H:nitrate reductase

Campbell, W. H. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000847 · Cited by 182 · see citing works

Biosynthesis of Proteins Incorporating a Versatile Set of Phenylalanine Analogues

Kirshenbaum, K., Carrico, I. S., & Tirrell, D. A. (2002) · ChemBioChem · doi:10.1002/1439-7633(20020301)3:2/3 · Cited by 172 · see citing works

Structural Basis of Eukaryotic Nitrate Reduction: Crystal Structures of the Nitrate Reductase Active Site

Fischer-Schrader, 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 157 · see citing works

Direct Studies on the Electron Transfer Sequence in Xanthine Oxidase by Electron Paramagnetic Resonance Spectroscopy

Bray, R. C., Palmer, G., & Beinert, H. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93903-7 · Cited by 155 · see citing works

The redox protein construction kit: pre-last universal common ancestor evolution of energy-conserving enzymes

Baymann, F., Lebrun, É., Brugna, M., Schoepp‐Cothenet, B., Giudici‐Orticoni, M., & Nitschke, W. (2003) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2002.1184 · Cited by 149 · see citing works

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 · see citing works

The 1.3 Å Crystal Structure ofRhodobacter sphaeroidesDimethyl Sulfoxide Reductase Reveals Two Distinct Molybdenum Coordination Environments

Li, H., Temple, C. A., Rajagopalan, K. V., & Schindelin, H. (2000) · Journal of the American Chemical Society · doi:10.1021/ja000643e · Cited by 139 · see citing works

The Crystal Structure of Plant Sulfite Oxidase Provides Insights into Sulfite Oxidation in Plants and Animals

Schrader, N., Fischer-Schrader, K., Theis, K. W., Mendel, R. R., Schwarz, G., & Kisker, C. (2003) · Structure · doi:10.1016/j.str.2003.09.001 · Cited by 138 · see citing works

Plant Sulfite Oxidase as Novel Producer of H2O2

Hänsch, R., Lang, C., Riebeseel, E., Lindigkeit, R., Geßler, A., Rennenberg, H., & Mendel, R. R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513054200 · Cited by 135 · see citing works

Molecular Basis of Intramolecular Electron Transfer in Sulfite-oxidizing Enzymes Is Revealed by High Resolution Structure of a Heterodimeric Complex of the Catalytic Molybdopterin Subunit and a c-Type Cytochrome Subunit

Kappler, U., & Bailey, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503237200 · Cited by 124 · see citing works

Spectropotentiometric and Structural Analysis of the Periplasmic Nitrate Reductase from Escherichia coli

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

Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth coordination of the catalytic molybdenum

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

Biochemical and Spectroscopic Characterization of the Human Mitochondrial Amidoxime Reducing Components hmARC-1 and hmARC-2 Suggests the Existence of a New Molybdenum Enzyme Family in Eukaryotes

Wahl, B., Reichmann, D., Niks, D., Krompholz, N., Havemeyer, A., Clement, B., Meßerschmidt, T., Rothkegel, M., Biester, H., Hille, R., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.169532 · Cited by 115 · see citing works

Molybdenum 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 114 · see citing works

On the mechanism of action of xanthine oxidase. Evidence in support of an oxo transfer mechanism in the molybdenum-containing hydroxylases.

Hille, R., & Sprecher, H. W. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60902-0 · Cited by 113 · see citing works

Structural 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 · see citing works

STUDIES ON URIC ACID AND RELATED COMPOUNDS

Bergmann, F., & Dikstein, S. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65076-8 · Cited by 106 · see citing works

Theoretical Studies on Models for the Oxo-Transfer Reaction of Dioxomolybdenum Enzymes

Pietsch, M. A., & Hall, M. B. (1996) · Inorganic Chemistry · doi:10.1021/ic951044p · Cited by 104 · see citing works

THE CRYSTAL STRUCTURE OF RHODOBACTER SPHAEROIDES DIMETHYLSULFOXIDE REDUCTASE REVEALS TWO DISTINCT MOLYBDENUM COORDINATION ENVIRONMENTS.

Li, H., Temple, K. L., Rajagopalan, K. V., & Schindelin, H. (2000) · Worldwide Protein Data Bank · doi:10.2210/pdb1eu1/pdb · Cited by 104 · see citing works

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 · see citing works

The Crystal Structure of Cupriavidus necator Nitrate Reductase in Oxidized and Partially Reduced States

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 · see citing works

Regulation of plant NR activity by reversible phosphorylation, 14-3-3 proteins and proteolysis

MacKintosh, C., & Meek, S. E. M. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000848 · Cited by 93 · see citing works

Oxo Transfer Reactions Mediated by Bis(dithiolene)tungsten Analogues of the Active Sites of Molybdoenzymes in the DMSO Reductase Family: Comparative Reactivity of Tungsten and Molybdenum

Sung, K.-M., & Holm, R. H. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0036559 · Cited by 92 · see citing works

Electron-paramagnetic-resonance parameters of molybdenum(V) in sulphite oxidase from chicken liver

Lamy, M. T., Gutteridge, S., & Bary, R. C. (1980) · Biochemical Journal · doi:10.1042/bj1850397 · Cited by 90 · see citing works

Cell biology of molybdenum

Mendel, R. R. (2009) · BioFactors · doi:10.1002/biof.55 · Cited by 89 · see citing works

Structural and Biochemical Characterization of a Quinol Binding Site of Escherichia coli Nitrate Reductase A

Bertero, M. G., Rothery, R. A., Boroumand, N., Palak, M., Blasco, F., Ginet, N., Weiner, J. H., & Strynadka, N. C. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410457200 · Cited by 88 · see citing works

Reduction of<i>N</i>ω-hydroxy-<scp>L</scp>-arginine by the mitochondrial amidoxime reducing component (mARC)

Kotthaus, J., Wahl, B., Havemeyer, A., Kotthaus, J., Schade, D., Garbe-Schönberg, D., Mendel, R., Bittner, F., & Clement, B. (2011) · Biochemical Journal · doi:10.1042/bj20100960 · Cited by 88 · see citing works

Spectroscopic studies of the molybdenum-containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans.

Bastian, N. R., Kay, C., Barber, M. J., & Rajagopalan, K. V. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52399-1 · Cited by 86 · 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

Paramagnetic Active Site Models for the Molybdenum−Copper Carbon Monoxide Dehydrogenase

Gourlay, C., Nielsen, D. J., White, J. M., Knottenbelt, S. Z., Kirk, M. L., & Young, C. G. (2006) · Journal of the American Chemical Society · doi:10.1021/ja056500f · Cited by 86 · see citing works

‘Rapidly Appearing’ molybdenum electron-paramagnetic-resonance signals from reduced xanthine oxidase

Bray, R. C., & Vänngård, T. (1969) · Biochemical Journal · doi:10.1042/bj1140725 · Cited by 85 · see citing works

Studies on Xanthine Oxidase

Dixon, M., & Thurlow, S. (1924) · Biochemical Journal · doi:10.1042/bj0180971 · Cited by 84 · see citing works

Comparative genomics and evolution of molybdenum utilization

Zhang, Y., Rump, S., & Gladyshev, V. N. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.02.016 · Cited by 83 · see citing works

Binding of Sulfurated Molybdenum Cofactor to the C-terminal Domain of ABA3 from Arabidopsis thaliana Provides Insight into the Mechanism of Molybdenum Cofactor Sulfuration

Wollers, S., Heidenreich, T., Zarepour, M., Zachmann, D. W., Kraft, C., Zhao, Y., Mendel, R. R., & Bittner, F. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708549200 · Cited by 83 · see citing works

Alteration of the iron-sulfur cluster composition of Escherichia coli dimethyl sulfoxide reductase by site-directed mutagenesis

Rothery, R. A., & Weiner, J. H. (1991) · Biochemistry · doi:10.1021/bi00098a003 · Cited by 82 · see citing works

A Combined QM/MM Study on the Reductive Half-Reaction of Xanthine Oxidase: Substrate Orientation and Mechanism

Metz, S., & Thiel, W. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9045394 · Cited by 81 · see citing works

Catalytic Reduction of a Tetrahydrobiopterin Radical within Nitric-oxide Synthase

Wei, C., Wang, Z., Tejero, J., Yang, Y., Hemann, C. F., Hille, R., & Stuehr, D. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709250200 · Cited by 74 · see citing works

Quantum chemical modeling of CO oxidation by the active site of molybdenum CO dehydrogenase

Siegbahn, P. E. M., & Shestakov, A. F. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20230 · Cited by 74 · see citing works

The Reaction Mechanism of Xanthine Oxidase: Evidence for Two-Electron Chemistry Rather Than Sequential One-Electron Steps

Stockert, A., Shinde, S. S., Anderson, R. F., & Hille, R. (2002) · Journal of the American Chemical Society · doi:10.1021/ja027388d · Cited by 73 · see citing works

The Role of Active Site Glutamate Residues in Catalysis of Rhodobacter capsulatus Xanthine Dehydrogenase

Leimkühler, S., Stockert, A., Igarashi, K., Nishino, T., & Hille, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405778200 · Cited by 73 · see citing works

Catalysis of the Direct Transfer of Oxygen from Nicotinamide N-Oxide to Xanthine by Xanthine Oxidase

Murray, K. N., Watson, J. G., & Chaykin, S. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99716-4 · Cited by 69 · see citing works

Structure of a Xanthine Oxidase-Related 4-Hydroxybenzoyl-CoA Reductase with an Additional [4Fe-4S] Cluster and an Inverted Electron Flow

Unciuleac, M., Warkentin, E., Page, C. C., Boll, M., & Ermler, U. (2004) · Structure · doi:10.1016/j.str.2004.10.008 · Cited by 69 · see citing works

The fourth mammalian molybdenum enzyme mARC: current state of research

Havemeyer, A., Lang, J., & Clement, B. (2011) · Drug Metabolism Reviews · doi:10.3109/03602532.2011.608682 · Cited by 67 · see citing works

The reductive half-reaction of xanthine oxidase. Identification of spectral intermediates in the hydroxylation of 2-hydroxy-6-methylpurine.

McWhirter, R. B., & Hille, R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54343-x · Cited by 66 · see citing works

Molecular Mechanism of 14-3-3 Protein-mediated Inhibition of Plant Nitrate Reductase

Lambeck, I., Fischer-Schrader, K., Niks, D., Roeper, J., Chi, J.-C., Hille, R., & Schwarz, G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.323113 · Cited by 66 · see citing works

MOSC domains: ancient, predicted sulfur-carrier domains, present in diverse metal–sulfur cluster biosynthesis proteins including Molybdenum cofactor sulfurases

Anantharaman, V., & Aravind, L. (2002) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2002.tb11028.x · Cited by 66 · see citing works

YcbX and yiiM, two novel determinants for resistance of Escherichia coli to N‐hydroxylated base analogues

Kozmin, S. G., Leroy, P., Pavlov, Y. I., & Schaaper, R. M. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06128.x · Cited by 64 · see citing works

The mechanism of Mo-/Cu-dependent CO dehydrogenase

Hofmann, M., Kassube, J. K., & Graf, T. (2005) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-005-0661-5 · Cited by 63 · see citing works

Kinetic Analysis of 14-3-3-Inhibited Arabidopsis thaliana Nitrate Reductase

Lambeck, I., Chi, J.-C., Krizowski, S., Mueller, S., Mehlmer, N., Teige, M., Fischer-Schrader, K., & Schwarz, G. (2010) · Biochemistry · doi:10.1021/bi1003487 · Cited by 62 · see citing works

A Theoretical Study of the Primary Oxo Transfer Reaction of a Dioxo Molybdenum(VI) Compound with Imine Thiolate Chelating Ligands: A Molybdenum Oxotransferase Analogue

Thomson, L. M., & Hall, M. B. (2001) · Journal of the American Chemical Society · doi:10.1021/ja003258y · Cited by 62 · see citing works

The Reductive Half-reaction of Xanthine Oxidase

Kim, J. H., Ryan, M. G., Knaut, H., & Hille, R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.12.6771 · Cited by 61 · see citing works

35 GHz ENDOR Characterization of the “Very Rapid” Signal of Xanthine Oxidase Reacted with 2-Hydroxy-6-methylpurine (13C8): Evidence against Direct Mo−C8 Interaction

Manikandan, P., Choi, E.-Y., Hille, R., & Hoffman, B. M. (2001) · Journal of the American Chemical Society · doi:10.1021/ja003894w · Cited by 61 · see citing works

FeII/α-ketoglutarate hydroxylases involved in nucleobase, nucleoside, nucleotide, and chromatin metabolism

Simmons, J. M., Müller, T., & Hausinger, R. P. (2008) · Dalton Transactions · doi:10.1039/b803512a · Cited by 60 · see citing works

Interaction of an Engineered [3Fe-4S] Cluster with a Menaquinol Binding Site of Escherichia coli DMSO Reductase

Rothery, R. A., & Weiner, J. H. (1996) · Biochemistry · doi:10.1021/bi951584y · Cited by 57 · see citing works

The Mo-Se active site of nicotinate dehydrogenase

Wagener, N., Pierik, A. J., Ibdah, A., Hille, R., & Dobbek, H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902210106 · Cited by 57 · see citing works

Sulfur K-Edge X-ray Absorption Spectroscopy and Density Functional Calculations on Mo(IV) and Mo(VI)═O Bis-dithiolenes: Insights into the Mechanism of Oxo Transfer in DMSO Reductase and Related Functional Analogues

Tenderholt, A. L., Wang, J., Szilagyi, R. K., Holm, R. H., Hodgson, K. O., Hedman, B., & Solomon, E. I. (2010) · Journal of the American Chemical Society · doi:10.1021/ja910369c · Cited by 52 · see citing works

Investigation of the coordination structures of the molybdenum(v) sites of sulfite oxidizing enzymes by pulsed EPR spectroscopy

Enemark, J. H., Astashkin, A. V., & Raitsimring, A. M. (2006) · Dalton Transactions · doi:10.1039/b602919a · Cited by 50 · see citing works

Crystal Structures of Urate Bound Form of Xanthine Oxidoreductase: Substrate Orientation and Structure of the Key Reaction Intermediate

Okamoto, K., Kawaguchi, Y., Eger, B. T., PAI, E. F., & Nishino, T. (2010) · Journal of the American Chemical Society · doi:10.1021/ja1077574 · Cited by 49 · see citing works

Structural and Electron Paramagnetic Resonance (EPR) Studies of Mononuclear Molybdenum Enzymes from Sulfate-Reducing Bacteria

Brondino, 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 49 · see citing works

Identification of a Rhodobacter capsulatus l -Cysteine Desulfurase That Sulfurates the Molybdenum Cofactor When Bound to XdhC and before Its Insertion into Xanthine Dehydrogenase

Neumann‐Schaal, M., Stöcklein, W., Walburger, A., Magalon, A., & Leimkühler, S. (2007) · Biochemistry · doi:10.1021/bi700630p · Cited by 48 · see citing works

Reaction of the Molybdenum- and Copper-Containing Carbon Monoxide Dehydrogenase from Oligotropha carboxydovorans with Quinones

Wilcoxen, J., Zhang, B., & Hille, R. (2011) · Biochemistry · doi:10.1021/bi1017182 · Cited by 48 · see citing works

The Role of Arginine 310 in Catalysis and Substrate Specificity in Xanthine Dehydrogenase from Rhodobacter capsulatus

Pauff, J. M., Hemann, C. F., Jünemann, N., Leimkühler, S., & Hille, R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700364200 · Cited by 48 · see citing works

The Chlamydomonas reinhardtii Molybdenum Cofactor Enzyme crARC Has a Zn-Dependent Activity and Protein Partners Similar to Those of Its Human Homologue

Chamizo‐Ampudia, A., Galván, A., Fernández, E. M., & Llamas, Á. (2011) · Eukaryotic Cell · doi:10.1128/ec.05096-11 · Cited by 48 · see citing works

Molybdenum enzymes

Hille, R. (1999) · Essays in Biochemistry · doi:10.1042/bse0340125 · Cited by 47 · see citing works

Structure of the Molybdenum Site in YedY, a Sulfite Oxidase Homologue from Escherichia coli

Havelius, K. G. V., Reschke, S., Horn, S., Döring, A., Niks, D., Hille, R., Schulzke, C., Leimkühler, S., & Haumann, M. (2010) · Inorganic Chemistry · doi:10.1021/ic101291j · Cited by 43 · see citing works

The Mechanism of Assembly and Cofactor Insertion into Rhodobacter capsulatus Xanthine Dehydrogenase

Schumann, S., Saggu, M., Möller, N., Anker, S. D., Lendzian, F., Hildebrandt, P., & Leimkühler, S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709894200 · Cited by 42 · see citing works

Structures of the Mo(V) Forms of Sulfite Oxidase from Arabidopsis thaliana by Pulsed EPR Spectroscopy

Astashkin, A. V., Hood, B. L., Feng, C., Hille, R., Mendel, R. R., Raitsimring, A. M., & Enemark, J. H. (2005) · Biochemistry · doi:10.1021/bi051220y · Cited by 41 · see citing works

Comparative Kinetics and Mechanism of Oxygen and Sulfur Atom Transfer Reactions Mediated by Bis(dithiolene) Complexes of Molybdenum and Tungsten

Wang, J., Kryatova, O. P., Rybak-Akimova, E. V., & Holm, R. H. (2004) · Inorganic Chemistry · doi:10.1021/ic040087f · Cited by 41 · see citing works

Spectroscopic and Electronic Structure Studies of a Dimethyl Sulfoxide Reductase Catalytic Intermediate: Implications for Electron- and Atom-Transfer Reactivity

Mtei, R. P., Lyashenko, G., Stein, B. W., Rubie, N. D., Hille, R., & Kirk, M. L. (2011) · Journal of the American Chemical Society · doi:10.1021/ja109178q · Cited by 40 · see citing works

The hpx Genetic System for Hypoxanthine Assimilation as a Nitrogen Source in Klebsiella pneumoniae : Gene Organization and Transcriptional Regulation

de la Riva, L., Badı́a, J., Aguilar, J., Bender, R. A., & Baldomà, L. (2008) · Journal of Bacteriology · doi:10.1128/jb.01022-08 · Cited by 40 · see citing works

Oxidative Half-reaction of Arabidopsis thaliana Sulfite Oxidase

Byrne, R. S., Hänsch, R., Mendel, R. R., & Hille, R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.067355 · Cited by 40 · see citing works

Mechanistic Studies of Rhodobacter sphaeroides Me2SO Reductase

Cobb, N. J., Conrads, T. P., & Hille, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412050200 · Cited by 38 · see citing works

Purine Utilization byKlebsiella oxytocaM5al: Genes for Ring-Oxidizing and -Opening Enzymes

Pope, S. D., Chen, L., & Stewart, V. J. (2008) · Journal of Bacteriology · doi:10.1128/jb.01281-08 · Cited by 38 · see citing works

Molybdenum cofactor-dependent resistance to N-hydroxylated base analogs in Escherichia coli is independent of MobA function

Kozmin, S. G., & Schaaper, R. M. (2007) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2006.12.005 · Cited by 34 · see citing works

Substitution of Silver for Copper in the Binuclear Mo/Cu Center of Carbon Monoxide Dehydrogenase from Oligotropha carboxidovorans

Wilcoxen, J., Snider, S., & Hille, R. (2011) · Journal of the American Chemical Society · doi:10.1021/ja205073j · Cited by 34 · see citing works

Direct Detection and Characterization of Chloride in the Active Site of the Low-pH Form of Sulfite Oxidase Using Electron Spin Echo Envelope Modulation Spectroscopy, Isotopic Labeling, and Density Functional Theory Calculations

Klein, E. L., Astashkin, A. V., Ganyushin, D., Riplinger, C., Johnson-Winters, K. L., Neese, F., & Enemark, J. H. (2009) · Inorganic Chemistry · doi:10.1021/ic801787s · Cited by 33 · see citing works

The Small Subunit AroB of Arsenite Oxidase

Duval, S., Santini, J. M., Nitschke, W., Hille, R., & Schoepp‐Cothenet, B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.113811 · Cited by 32 · see citing works

Tautomerization of the substrate heterocycle in the course of the reaction of xanthine oxidase

Ilich, P., & Hille, R. (1997) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(97)05654-5 · Cited by 30 · see citing works

Spectroscopic Characterization of YedY: The Role of Sulfur Coordination in a Mo(V) Sulfite Oxidase Family Enzyme Form

Yang, J., Rothery, R. A., Sempombe, J., Weiner, J. H., & Kirk, M. L. (2009) · Journal of the American Chemical Society · doi:10.1021/ja903087k · Cited by 29 · see citing works

Role for CysJ Flavin Reductase in Molybdenum Cofactor-Dependent Resistance of Escherichia coli to 6- N -Hydroxylaminopurine

Kozmin, S. G., Wang, J., & Schaaper, R. M. (2010) · Journal of Bacteriology · doi:10.1128/jb.01438-09 · Cited by 28 · see citing works

The Molybdenum Centers of Xanthine Oxidase and Xanthine Dehydrogenase

Ryan, M. G., Ratnam, K., & Hille, R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.33.19209 · Cited by 27 · see citing works

Sulfite: Cytochrome c Oxidoreductase

Howell, L. G., & Fridovich, I. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94511-4 · Cited by 27 · see citing works

Spectroscopic and Electronic Structure Studies Probing Covalency Contributions to C–H Bond Activation and Transition-State Stabilization in Xanthine Oxidase

Sempombe, J., Stein, B. W., & Kirk, M. L. (2011) · Inorganic Chemistry · doi:10.1021/ic201477n · Cited by 26 · see citing works

Characterization of Chloride-Depleted Human Sulfite Oxidase by Electron Paramagnetic Resonance Spectroscopy: Experimental Evidence for the Role of Anions in Product Release

Rajapakshe, A., Johnson-Winters, K. L., Nordstrom, A. R., Meyers, K. T., Emesh, S., Astashkin, A. V., & Enemark, J. H. (2010) · Biochemistry · doi:10.1021/bi902172n · Cited by 24 · see citing works

Density-functional theory models of xanthine oxidoreductase activity: comparison of substrate tautomerization and protonation

Bayse, C. A. (2009) · Dalton Transactions · doi:10.1039/b821878a · Cited by 24 · see citing works

Molybdenum Site Structure of Escherichia coli YedY, a Novel Bacterial Oxidoreductase

Pushie, M. J., Doonan, C. J., Moquin, K., Weiner, J. H., Rothery, R. A., & George, G. N. (2010) · Inorganic Chemistry · doi:10.1021/ic101280m · Cited by 23 · see citing works

Nature of Halide Binding to the Molybdenum Site of Sulfite Oxidase

Pushie, M. J., Doonan, C. J., Wilson, H. L., Rajagopalan, K. V., & George, G. N. (2011) · Inorganic Chemistry · doi:10.1021/ic201030u · Cited by 8 · see citing works

How biology handles nitrite

Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401 · see citing works

The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity

Lehnert, N., Kim, E., Dong, H. T., Harland, J. B., Hunt, A. P., Manickas, E. C., Oakley, K. M., Pham, J., Reed, G. C., & Alfaro, V. S. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00253 · Cited by 277 · see citing works

Solids Go Bio: Inorganic Nanoparticles as Enzyme Mimics

Ragg, R., Tahir, M. N., & Tremel, W. (2015) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201501237 · Cited by 193 · see citing works

Molybdenum Trioxide Nanoparticles with Intrinsic Sulfite Oxidase Activity

Ragg, R., Natálio, F., Tahir, M. N., Janssen, H., Kashyap, A., Strand, D. J., Strand, S., & Tremel, W. (2014) · ACS Nano · doi:10.1021/nn501235j · Cited by 179 · see citing works

Molybdenum metabolism in plants and crosstalk to iron

Bittner, F. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00028 · Cited by 171 · see citing works

Secondary-Sphere Effects in Molecular Electrocatalytic CO2 Reduction

Nichols, A. W., & Machan, C. W. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00397 · Cited by 169 · see citing works

Molybdenum 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 159 · see citing works

Mechanisms of nitrite bioactivation

Kim-Shapiro, D. B., & Gladwin, M. T. (2014) · Nitric Oxide · doi:10.1016/j.niox.2013.11.002 · Cited by 157 · see citing works

Iron chaperones PCBP1 and PCBP2 mediate the metallation of the dinuclear iron enzyme deoxyhypusine hydroxylase

Frey, A. G., Nandal, A., Park, J. H., Smith, P. M., Yabe‐Wada, T., Ryu, M., Ghosh, M. C., Lee, J., Rouault, T. A., Park, M. H., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402732111 · Cited by 136 · see citing works

Bacterial steroid hydroxylases: enzyme classes, their functions and comparison of their catalytic mechanisms

Szaleniec, M., Wojtkiewicz, A. M., Bernhardt, R., Borowski, T., & Donova, M. V. (2018) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-018-9239-3 · Cited by 110 · see citing works

Genetic basis for the cooperative bioactivation of plant lignans by Eggerthella lenta and other human gut bacteria

Bess, E. N., Bisanz, J. E., Yarza, F., Bustion, A. E., Rich, B. E., Li, X., Kitamura, S., Waligurski, E., Ang, Q. Y., Alba, D., et al. (2019) · Nature Microbiology · doi:10.1038/s41564-019-0596-1 · Cited by 105 · see citing works

A Step into the Future: Applications of Nanoparticle Enzyme Mimics

Korschelt, K., Tahir, M. N., & Tremel, W. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201800384 · Cited by 102 · see citing works

Mechanistic insights into xanthine oxidoreductase from development studies of candidate drugs to treat hyperuricemia and gout

Nishino, T., & Okamoto, K. (2014) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-014-1210-x · Cited by 99 · see citing works

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 86 · see citing works

Carbon Monoxide. Toxic Gas and Fuel for Anaerobes and Aerobes: Carbon Monoxide Dehydrogenases

Jeoung, J., Fesseler, J., Goetzl, S., & Dobbek, H. (2014) · Metal ions in life sciences · doi:10.1007/978-94-017-9269-1_3 · Cited by 65 · see citing works

Structural basis of enzymatic benzene ring reduction

Weinert, T., Huwiler, S. G., Kung, J. W., Weidenweber, S., Hellwig, P., Stärk, H., Biskup, T., Weber, S., Cotelesage, J. J. H., George, G. N., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1849 · Cited by 63 · see citing works

Ethylbenzene Dehydrogenase and Related Molybdenum Enzymes Involved in Oxygen-Independent Alkyl Chain Hydroxylation

Heider, J., Szaleniec, M., Sünwoldt, K., & Boll, M. (2016) · Microbial Physiology · doi:10.1159/000441357 · Cited by 63 · see citing works

Bioinspired functional analogs of the active site of molybdenum enzymes: Intermediates and mechanisms

Heinze, K. (2015) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2015.04.010 · Cited by 61 · see citing works

MoOx quantum dots with peroxidase-like activity on microfluidic paper-based analytical device for rapid colorimetric detection of H2O2 released from PC12 cells

Liu, M., Li, S., Huang, D., Xu, Z., Wu, Y., Lei, Y., & Liu, A. (2019) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2019.127512 · Cited by 55 · see citing works

Electrochemical evidence that pyranopterin redox chemistry controls the catalysis of YedY, a mononuclear Mo enzyme

Adamson, H., Simonov, A. N., Kierzek, M., Rothery, R. A., Weiner, J. H., Bond, A. M., & Parkin, A. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516869112 · Cited by 53 · see citing works

Tungstoenzymes: Occurrence, Catalytic Diversity and Cofactor Synthesis

Seelmann, C. S., Willistein, M., Heider, J., & Boll, M. (2020) · Inorganics · doi:10.3390/inorganics8080044 · Cited by 52 · see citing works

Nanotechnology Tools Enabling Biological Discovery

Salvador-Morales, C., & Grodzinski, P. A. (2022) · ACS Nano · doi:10.1021/acsnano.1c10635 · Cited by 51 · see citing works

Dioxomolybdenum(VI) and ‐tungsten(VI) Complexes with Multidentate Aminobisphenol Ligands as Catalysts for Olefin Epoxidation

Dupé, A., Hossain, M. K., Schachner, J. A., Belaj, F., Lehtonen, A., Nordlander, E., & Zanetti, N. C. (2015) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201500055 · Cited by 48 · see citing works

Bioinorganic modeling chemistry of carbon monoxide dehydrogenases: description of model complexes, current status and possible future scopes

Majumdar, A. (2014) · Dalton Transactions · doi:10.1039/c4dt00729h · Cited by 45 · see citing works

Activation of molecular oxygen by a molybdenum complex for catalytic oxidation

Dupé, A., Judmaier, M. E., Belaj, F., Zangger, K., & Zanetti, N. C. (2015) · Dalton Transactions · doi:10.1039/c5dt02931g · Cited by 44 · see citing works

Roles of Molybdenum in Plants and Improvement of Its Acquisition and Use Efficiency

Tejada‐Jiménez, M., Chamizo‐Ampudia, A., Llamas, Á., Galván, A., & Fernández, E. M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-812104-7.00009-5 · Cited by 44 · see citing works

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 40 · see citing works

Structural and functional models in molybdenum and tungsten bioinorganic chemistry: description of selected model complexes, present scenario and possible future scopes

Majumdar, A. (2014) · Dalton Transactions · doi:10.1039/c4dt00631c · Cited by 37 · see citing works

Structure and Function of the Unusual Tungsten Enzymes Acetylene Hydratase and Class II Benzoyl-Coenzyme A Reductase

Boll, M., Einsle, O., Ermler, U., Kroneck, P. M. H., & Ullmann, G. M. (2016) · Microbial Physiology · doi:10.1159/000440805 · Cited by 37 · see citing works

Synthesis and Characterization of a Well-Defined Carbon Nanohorn-Supported Molybdenum Dioxo Catalyst by SMART-EM Imaging. Surface Structure at the Atomic Level

Kratish, Y., Nakamuro, T., Liu, Y., Li, J., Tomotsuka, I., Harano, K., Nakamura, E., & Marks, T. J. (2020) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.20200299 · Cited by 36 · see citing works

Electronic structure contributions to reactivity in xanthine oxidase family enzymes

Stein, B. W., & Kirk, M. L. (2014) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-014-1212-8 · Cited by 35 · see citing works

The chaperone FdsC for Rhodobacter capsulatus formate dehydrogenase binds the bis‐molybdopterin guanine dinucleotide cofactor

Böhmer, N., Hartmann, T., & Leimkühler, S. (2014) · FEBS Letters · doi:10.1016/j.febslet.2013.12.033 · Cited by 34 · see citing works

New asymmetric Schiff base ligand derived from allylamine and 2,3-dihydroxybenzaldehyde and its molybdenum(VI) complex: Synthesis, characterization, crystal structures, computational studies and antibacterial activity together with synergistic effect against Pseudomonas aeroginosa PTTC 1570

Rudbari, H. A., Khorshidifard, M., Askari, B., Habibi, N., & Brunò, G. (2015) · Polyhedron · doi:10.1016/j.poly.2015.07.060 · Cited by 33 · see citing works

Deoxygenation reactions in organic synthesis catalyzed by dioxomolybdenum( vi ) complexes

Suárez‐Pantiga, S., & Sanz, R. (2021) · Organic & Biomolecular Chemistry · doi:10.1039/d1ob01939b · Cited by 33 · see citing works

Inorganic nitrite bioactivation and role in physiological signaling and therapeutics

Amdahl, M. B., DeMartino, A. W., & Gladwin, M. T. (2019) · Biological Chemistry · doi:10.1515/hsz-2019-0349 · Cited by 31 · see citing works

Oxygen Atom Transfer Reactivity of Molybdenum(VI) Complexes Employing Pyrimidine- and Pyridine-2-thiolate Ligands

Ehweiner, M. A., Wiedemaier, F., Belaj, F., & Zanetti, N. C. (2020) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.0c02412 · Cited by 31 · see citing works

“Repurposing” of Xanthine Oxidoreductase as a Nitrite Reductase: A New Paradigm for Therapeutic Targeting in Hypertension

Khambata, R. S., Ghosh, S. M., & Ahluwalia, A. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6254 · Cited by 30 · see citing works

Selective Reduction of Aqueous Nitrate to Ammonium with an Electropolymerized Chromium Molecular Catalyst

Askari, M. J., Kallick, J. D., & McCrory, C. C. L. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c12783 · Cited by 26 · see citing works

One Electron Reduced Square Planar Bis(benzene-1,2-dithiolato) Copper Dianionic Complex and Redox Switch by O2/HO–

Maiti, B. K., Maia, L. B., Pal, K., Pakhira, B., Avilés, T., Moura, I., Pauleta, S. R., Núñez, J. L., Rizzi, A. C., Brondino, C. D., et al. (2014) · Inorganic Chemistry · doi:10.1021/ic501742j · Cited by 25 · see citing works

Dioxidomolybdenum(VI) Complexes Containing Ligands with the Bipyrrolidine Backbone as Efficient Catalysts for Olefin Epoxidation

Mayilmurugan, R., Traar, P., Schachner, J. A., Volpe, M., & Zanetti, N. C. (2013) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201300258 · Cited by 24 · see citing works

‘Come into the fold’: A comparative analysis of bacterial redox enzyme maturation protein members of the NarJ subfamily

Chan, C. S., Bay, D. C., Leach, T., Winstone, T. M. L., Kuzniatsova, L., Tran, V. A., & Turner, R. J. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.08.020 · Cited by 22 · see citing works

Mechanism of the Molybdenum-Mediated Cadogan Reaction

Reis, M. C., Marín‐Luna, M., López, C. S., & Faza, O. N. (2018) · ACS Omega · doi:10.1021/acsomega.8b01278 · Cited by 22 · see citing works

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 · see citing works

Mild, Selective Sulfoxidation with Molybdenum(VI) cis -Dioxo Catalysts

Cantwell, K. E., Fanwick, P. E., & Abu‐Omar, M. M. (2017) · ACS Omega · doi:10.1021/acsomega.7b00292 · Cited by 21 · see citing works

Synthesis, characterization and biomedical activities of molybdenum complexes of tridentate Schiff base ligands. Crystal and molecular structure of [MoO2(L10)(DMSO)] and [MoO2(L11)(DMSO)]

Rakshit, S., Palit, D., Hazari, S. K. S., Rabi, S., Roy, T. G., Olbrich, F., & Rehder, D. (2016) · Polyhedron · doi:10.1016/j.poly.2016.05.053 · Cited by 20 · see citing works

Remote Charge Effects on the Oxygen-Atom-Transfer Reactivity and Their Relationship to Molybdenum Enzymes

Paudel, J., Pokhrel, A., Kirk, M. L., & Li, F. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b03093 · Cited by 19 · see citing works

Bimetallic cis-dioxomolybdenum(VI) complex containing hydrazone ligand: Syntheses, crystal structure and catalytic studies

Kurbah, S. D., Kumar, A., Syiemlieh, I., Asthana, M., & Lal, R. A. (2017) · Inorganic Chemistry Communications · doi:10.1016/j.inoche.2017.09.018 · Cited by 19 · see citing works

Dioxomolybdenum(VI) complexes of hydrazone phenolate ligands - syntheses and activities in catalytic oxidation reactions

Hossain, M. K., Plutenko, M. O., Schachner, J. A., Haukka, M., Zanetti, N. C., Fritsky, I. O., & Nordlander, E. (2021) · Journal of the Indian Chemical Society · doi:10.1016/j.jics.2021.100006 · Cited by 18 · see citing works

Tungsten Enzyme Using Hydrogen as an Electron Donor to Reduce Carboxylic Acids and NAD+

Winiarska, A., Hege, D., Gemmecker, Y., Kryściak‐Czerwenka, J., Seubert, A., Heider, J., & Szaleniec, M. (2022) · ACS Catalysis · doi:10.1021/acscatal.2c02147 · Cited by 17 · see citing works

Oxygen Atom Transfer Catalysis with Homogenous and Polymer‐Supported N,N‐ and N,N,O‐Heteroscorpionate Dioxidomolybdenum(VI) Complexes

Paul, T., Rodehutskors, P., Schmidt, J., & Burzlaff, N. I. (2016) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201600026 · Cited by 17 · see citing works

New magnetic supported hydrazone Schiff base dioxomolybdenum (VI) complex: An efficient nanocatalyst for epoxidation of cyclooctene and norbornene

Sarkheil, M., & Lashanizadegan, M. (2018) · Applied Organometallic Chemistry · doi:10.1002/aoc.4459 · Cited by 17 · see citing works

Oxo-carboxylato-molybdenum(vi) complexes possessing dithiolene ligands related to the active site of type II DMSOR family molybdoenzymes

Sugimoto, H., Sato, M., Giles, L. J., Asano, K., Suzuki, T., Kirk, M. L., & Itoh, S. (2013) · Dalton Transactions · doi:10.1039/c3dt51485d · Cited by 17 · see citing works

Dioxomolybdenum(VI) and -Tungsten(VI) Amino Bisphenolates as Epoxidation Catalysts

Peuronen, A., & Lehtonen, A. (2016) · Topics in Catalysis · doi:10.1007/s11244-016-0632-9 · Cited by 16 · see citing works

Discovery of a Gut Bacterial Pathway for Ergothioneine Catabolism

Feng, C., Yan, Q., Li, X., Zhao, H., Huang, H., & Zhang, X. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c09350 · Cited by 16 · see citing works

A Model for the Active-Site Formation Process in DMSO Reductase Family Molybdenum Enzymes Involving Oxido−Alcoholato and Oxido−Thiolato Molybdenum(VI) Core Structures

Sugimoto, H., Sato, M., Asano, K., Suzuki, T., Mieda, K., Ogura, T., Matsumoto, T., Giles, L. J., Pokhrel, A., Kirk, M. L., et al. (2016) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.5b02395 · Cited by 16 · see citing works

Oxygen atom transfer between DMSO and benzoin catalyzed by cis -dioxidomolybdenum( vi ) complexes of tetradentate Mannich bases

Maurya, M. R., Mengesha, B., Uprety, B., Jangra, N., Tomar, R., & Avecilla, F. (2018) · New Journal of Chemistry · doi:10.1039/c7nj03551a · Cited by 15 · see citing works

Selective and Efficient Detoxification of Sulfur Mustard Gas Analogues with H 2 O 2 Using Bioinspired Mo and W Dithiolene Catalysts

Tanriover, B., Subasinghe, S. M. S., & Mankad, N. P. (2024) · ACS Catalysis · doi:10.1021/acscatal.4c01979 · Cited by 13 · see citing works

Generation of Thiosulfate, Selenite, Dithiosulfite, Perthionitrite, Nitric Oxide, and Reactive Chalcogen Species by Binuclear Zinc(II)-Chalcogenolato/-Polychalcogenido Complexes

Atta, S., Mandal, A., & Majumdar, A. (2024) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.4c02527 · Cited by 13 · see citing works

TusA (YhhP) and IscS are required for molybdenum cofactor‐dependent base‐analog detoxification

Kozmin, S. G., Stepchenkova, E. I., & Schaaper, R. M. (2013) · MicrobiologyOpen · doi:10.1002/mbo3.108 · Cited by 13 · see citing works

The Challenging in silico Description of Carbon Monoxide Oxidation as Catalyzed by Molybdenum-Copper CO Dehydrogenase

Rovaletti, A., Bruschi, M., Moro, G., Cosentino, U., & Greco, C. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2018.00630 · Cited by 13 · see citing works

Electron transfer pathways and spin–spin interactions in Mo- and Cu-containing oxidoreductases

González, P. J., Rivas, M. G., Ferroni, F. M., Rizzi, A. C., & Brondino, C. D. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214202 · Cited by 11 · see citing works

EPR Spectroscopy on Mononuclear Molybdenum-Containing Enzymes

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

An Asymmetrically Substituted Aliphatic Bis-Dithiolene Mono-Oxido Molybdenum(IV) Complex With Ester and Alcohol Functions as Structural and Functional Active Site Model of Molybdoenzymes

Ahmadi, M., Fischer, C. E., Ghosh, A. C., & Schulzke, C. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00486 · Cited by 11 · see citing works

Effects of molybdenum sprays on the growth, yield and fruit quality of ‘Red Jonaprince’ apple trees

Wójcik, P. (2020) · Scientia Horticulturae · doi:10.1016/j.scienta.2020.109422 · Cited by 11 · see citing works

Catalytic oxidation of sulfides and alcohols by vanadium, molybdenum, and tungsten Schiff base complexes: A combined structural, spectral, and theoretical study

Fallah‐Mehrjardi, M., Kargar, H., Munawar, K. S., & Ashfaq, M. H. (2025) · Journal of Catalysis · doi:10.1016/j.jcat.2025.116441 · Cited by 10 · see citing works

Investigation of spectroscopic, crystallographic, thermal and antioxidant properties of mononuclear dioxomolybdenum(VI) complexes derived from a new symmetric bisthiocarbohydrazone

Kaya, Y. (2022) · Polyhedron · doi:10.1016/j.poly.2022.116151 · Cited by 10 · see citing works

Tungsten-containing enzymes

Paoletti, N. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-823974-2.00007-3 · Cited by 10 · see citing works

Oxocomplexes of Mo( vi ) and W( vi ) with 8-hydroxyquinoline-5-sulfonate in solution: structural studies and the effect of the metal ion on the photophysical behaviour

Ramos, M. L., Justino, L. L. G., Abreu, P. E., Fonseca, S. M., & Burrows, H. D. (2015) · Dalton Transactions · doi:10.1039/c5dt03473f · Cited by 10 · see citing works

YedY: A Mononuclear Molybdenum Enzyme with a Redox‐Active Ligand?

Lee, C. C., Sickerman, N. S., Hu, Y., & Ribbe, M. W. (2016) · ChemBioChem · doi:10.1002/cbic.201600004 · Cited by 10 · see citing works

Redox‐Controlled Stabilization of an Open‐Shell Intermediate in a Bioinspired Enzyme Model

Hanauer, K., Förster, C., & Heinze, K. (2018) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201800570 · Cited by 9 · see citing works

Mo@GAA-Fe 3 O 4 MNPs: a highly efficient and environmentally friendly heterogeneous magnetic nanocatalyst for the synthesis of polyhydroquinoline derivatives

Aghaei-Hashjin, M., Yahyazadeh, A., & Abbaspour‐Gilandeh, E. (2021) · RSC Advances · doi:10.1039/d1ra00396h · Cited by 9 · see citing works

Heme b quotas are low in Southern Ocean phytoplankton

Gledhill, M., Gerringa, L. J. A., Laan, P., & Timmermans, K. R. (2015) · Marine Ecology Progress Series · doi:10.3354/meps11345 · Cited by 9 · see citing works

[MoO 2 ] 2+ -Mediated Oxygen Atom Transfer via an Unusual Lewis Acid Mechanism

Reis, M. C., Marín‐Luna, M., López, C. S., & Faza, O. N. (2017) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.7b01529 · Cited by 9 · see citing works

Synthesis, Characterization, and Fluorescence Chemosensor Properties of a cis‐Dioxomolybdenum(VI) Complex Containing Multidentate Hydrazone Ligands

Kurbah, S. D., Kumar, A., Shangpung, S., Syiemlieh, I., Khongjoh, I., & Lal, R. A. (2017) · Zeitschrift für anorganische und allgemeine Chemie · doi:10.1002/zaac.201700100 · Cited by 9 · see citing works

Formation of Mono Oxo Molybdenum(IV) PNP Pincer Complexes: Interplay between Water and Molecular Oxygen

de Aguiar, S. R. M. M., Öztopcu, Ö., Troiani, A., de Petris, G., Weil, M., Stöger, B., Pittenauer, E., Allmaier, G. M., Veiros, L. F., & Kirchner, K. (2018) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201701413 · Cited by 8 · see citing works

Chemistry of oxidomolybdenum(IV) and -(VI) complexes with ONS donor ligands: Synthesis, computational evaluation and oxo-transfer reactions

Saswati, S., Roy, S., Dash, S. P., Acharyya, R., Kaminsky, W., Ugone, V., Garribba, E., Harris, C., Lowe, J. M., & Dinda, R. (2017) · Polyhedron · doi:10.1016/j.poly.2017.12.023 · Cited by 9 · see citing works

Iron-sulfur cluster-dependent enzymes and molybdenum-dependent reductases in the anaerobic metabolism of human gut microbes

Zahn, L. E., Gannon, P. M., & Rajakovich, L. J. (2024) · Metallomics · doi:10.1093/mtomcs/mfae049 · Cited by 8 · see citing works

Bioinspired Mo, W and V complexes bearing a highly hydroxyl-functionalized Schiff base ligand

Salonen, P., Peuronen, A., & Lehtonen, A. (2020) · Inorganica Chimica Acta · doi:10.1016/j.ica.2020.119414 · Cited by 8 · see citing works

Assembly pathway of a bacterial complex iron sulfur molybdoenzyme

Cherak, S. J., & Turner, R. J. (2017) · BioMolecular Concepts · doi:10.1515/bmc-2017-0011 · Cited by 8 · see citing works

The Genetic Basis for the Cooperative Bioactivation of Plant Lignans by a Human Gut Bacterial ConsortiumPreprint

Bess, E. N., Bisanz, J. E., Spanogiannopoulos, P., Ang, Q. Y., Bustion, A. E., Kitamura, S., Alba, D., Wolan, D. W., Koliwad, S. K., & Turnbaugh, P. J. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/357640 · Cited by 8 · see citing works

Cis- and trans molybdenum oxo complexes of a prochiral tetradentate aminophenolate ligand: Synthesis, characterization and oxotransfer activity

Hossain, M. K., Köhntopp, A., Haukka, M., Richmond, M. G., Lehtonen, A., & Nordlander, E. (2019) · Polyhedron · doi:10.1016/j.poly.2019.114312 · Cited by 7 · see citing works

Bringing Nitric Oxide to the Molybdenum World—A Personal Perspective

Maia, L. B. (2023) · Molecules · doi:10.3390/molecules28155819 · Cited by 7 · see citing works

Oxidovanadium( iv ), oxidomolybdenum( vi ) and cobalt( iii ) complexes of o-phenylenediamine derivatives: oxidative dehydrogenation and photoluminescence

Chaudhuri, S., Bera, S., Biswas, M. K., Roy, A. S., Weyhermüller, T., & Ghosh, P. (2014) · Inorganic Chemistry Frontiers · doi:10.1039/c3qi00103b · Cited by 7 · see citing works

Structural Basis of Thermal Stability of the Tungsten Cofactor Synthesis Protein MoaB from Pyrococcus furiosus

Havarushka, N., Fischer-Schrader, K., Lamkemeyer, T., & Schwarz, G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086030 · Cited by 7 · see citing works

The Reductive Half-reaction of Xanthine Dehydrogenase from Rhodobacter capsulatus

Hall, J. E., Reschke, S., Cao, H., Leimkühler, S., & Hille, R. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.603456 · Cited by 7 · see citing works

Biomimetic Studies of the Mo/Cu Active Site of CO Dehydrogenase

Mankad, N. P., & Ghosh, D. (2021) · Elsevier eBooks · doi:10.1016/b978-0-08-102688-5.00060-x · Cited by 6 · see citing works

Oxido-alcoholato/thiolato-molybdenum(VI) complexes with a dithiolene ligand generated by oxygen atom transfer to the molybdenum(IV) complexes

Sugimoto, H., Sato, M., Asano, K., Suzuki, T., Ogura, T., & Itoh, S. (2018) · Inorganica Chimica Acta · doi:10.1016/j.ica.2018.10.001 · Cited by 7 · see citing works

Unraveling the mechanism behind air instability in thin semiconducting polymer layers p-doped with molybdenum dithiolene complexes

Domschke, T. N., Bardagot, O., Benayad, A., Demadrille, R., Carella, A., Clerc, R., & Pereira, A. (2019) · Synthetic Metals · doi:10.1016/j.synthmet.2019.116251 · Cited by 6 · see citing works

Can Water Act as a Nucleophile in CO Oxidation Catalysed by Mo/Cu CO‐Dehydrogenase? Answers from Theory

Rovaletti, A., Moro, G., Cosentino, U., Ryde, U., & Greco, C. (2022) · ChemPhysChem · doi:10.1002/cphc.202200053 · Cited by 6 · see citing works

Influence of GTP on system specific chaperone – Twin arginine signal peptide interaction

Cherak, S. J., & Turner, R. J. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.08.079 · Cited by 5 · see citing works

Dioxomolybdenum(VI) complexes of 2-hydroxy-4-benzyloxybenzaldehyde thiosemicarbazones alkylated via N or S atoms. Synthesis, characterization, antioxidant and xanthine oxidase inhibition performance

Eğlence-Bakır, S., Şahın, M., Erdemir, E., Özyürek, M., & Ülküseven, B. (2023) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2023.136604 · Cited by 5 · see citing works

Catalytic conversion of isoelectronic CO and N2 molecules in the presence of hydrogen

Permyakov, E. A., & Kogan, V. M. (2023) · Russian Chemical Reviews · doi:10.59761/rcr5094 · Cited by 5 · see citing works

New solvated Mo(VI) complexes of isatin based asymmetric bisthiocarbohydrazones as potent bioactive agent: synthesis, DFT-molecular docking studies, biological activity evaluation and crystal structures

Kaya, Y., Erçağ, A., Kaya, S., Бериша, А., Akkaya, B., & Zorlu, Y. (2024) · BioMetals · doi:10.1007/s10534-024-00633-x · Cited by 5 · see citing works

Archaeal Mo-Containing Glyceraldehyde Oxidoreductase Isozymes Exhibit Diverse Substrate Specificities through Unique Subunit Assemblies

Wakagi, T., Nishimasu, H., Miyake, M., & Fushinobu, S. (2016) · PLoS ONE · doi:10.1371/journal.pone.0147333 · Cited by 5 · see citing works

A Synthetic Molybdenum Hydroxylase Compound That Cleaves C–H Bonds by Hydride Abstraction

Modappilappally, A. V., & Mankad, N. P. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c03753 · Cited by 3 · see citing works

Comparing {Mo2O5} and {V2O4} Cores in Aerobic Catalysts for Oxidative Alcohol Dehydrogenation

Cerritelli, J. E., Brown, J. R., Bussiere, M. M., Mdalel, T. B., Abdu, R. B., Choi, S., Rheingold, A. L., Bacon, J. W., & Doerrer, L. H. (2025) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.5c03009 · Cited by 4 · see citing works

Complementary hydrophobic interaction of the redox enzyme maturation protein NarJ with the signal peptide of the respiratory nitrate reductase NarG

Song, W. S., Kim, J.-H., Namgung, B., Cho, H. Y., Shin, H., Oh, H. B., Ha, N., & Yoon, S. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.129620 · Cited by 4 · see citing works

Mononuclear Molybdenum-Containing Enzymes

Maia, L. B., & Moura, J. J. G. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.13932-0 · Cited by 4 · see citing works

ONN donor half-salen ligands and their dioxomolybdenum(VI) complexes: Synthesis, crystal structure, experimental-theoretical characterizations and molecular docking studies

Portakal, E. D., Kaya, S., Бериша, А., Kaya, Y., Şahin, O., & Erçağ, A. (2025) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2025.141508 · Cited by 3 · see citing works

Reaction Pathway for the Aerobic Oxidation of Phosphines Catalyzed by Oxomolybdenum Salen Complexes

Rusmore, T. A., Lander, C., & Nicholas, K. M. (2023) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202300506 · Cited by 3 · see citing works

Molybdenum enzymes

Hille, R. (1999) · Essays in Biochemistry · doi:10.1042/bse0340125 · Cited by 47 · see citing works

Mechanistic aspects of molybdenum-containing enzymes

Hille, R., Rétey, J., Bartlewski‐Hof, U., Reichenbecher, W., & Schink, B. (1998) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(98)00037-0 · Cited by 80 · see citing works

Ab Initio and Density Functional Theory Applied to Models for the Oxo-Transfer Reaction of Dioxomolybdenum Enzymes

Zarić, S. D., & Hall, M. B. (1997) · Springer eBooks · doi:10.1007/978-94-011-5171-9_12

Molybdendium Enzymes and Models

Burgmayer, S. J. N. (2002) · Wiley eBooks · doi:10.1002/0471227617.eoc152

Mononuclear Molybdenum-Containing Enzymes

Maia, L. B., & Moura, J. J. G. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.13932-0 · Cited by 4 · see citing works