Synthetic Analogues and Reaction Systems Relevant to the Molybdenum and Tungsten Oxotransferases

Comprehensive Coordination Chemistry

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The mononuclear molybdenum enzymes

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The Mononuclear Molybdenum Enzymes

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Metal-centered oxygen atom transfer reactions

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Electron Paramagnetic Resonance of d Transition Metal Compounds

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

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Metal 1,2‐Dithiolene and Related Complexes

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Aconitase as iron–sulfur protein, enzyme, and iron-regulatory protein

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

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Structure of a Hyperthermophilic Tungstopterin Enzyme, Aldehyde Ferredoxin Oxidoreductase

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Molecular Basis of Proton Motive Force Generation: Structure of Formate Dehydrogenase-N

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

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

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Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination

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Molybdenum and tungsten in biology

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

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Metal Complexes Derived from cis ‐1,2‐dicyano‐1,2‐ethylenedithiolate and Bis(Trifluoromethyl)‐1,2‐dithiete

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Tungsten in biological systems

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The biologically relevant oxygen atom transfer chemistry of molybdenum: from synthetic analogue systems to enzymes

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Tungstoenzymes

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

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Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods

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The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway

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Structural and metabolic relationship between the molybdenum cofactor and urothione.

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Crystal Structure of Dimethyl Sulfoxide Reductase fromRhodobacter capsulatusat 1.88 Å Resolution

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

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

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Gene Sequence and the 1.8 Å Crystal Structure of the Tungsten-Containing Formate Dehydrogenase from Desulfovibrio gigas

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

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A thermodynamic scale for oxygen atom transfer reactions

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Bioinorganic Chemistry of Pterin-Containing Molybdenum and Tungsten Enzymes

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The high resolution crystal structure of DMSO reductase in complex with DMSO 1 1Edited by D. C. Rees

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Model for the active site of oxo-transfer molybdoenzymes: synthesis, structure, and properties

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Nickel Dithiolenes Revisited: Structures and Electron Distribution from Density Functional Theory for the Three-Member Electron-Transfer Series [Ni(S2C2Me2)2]0,1-,2-

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The inorganic biochemistry of molybdoenzymes

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Hydrocarbon oxidation by high-valent Group VI oxides

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Syntheses, structures, and spectroscopic properties of six-coordinate mononuclear oxo-molybdenum(V) complexes stabilized by the hydrotris(3,5-dimethyl-1-pyrazolyl)borate ligand

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Molybdenum-mediated oxygen-atom transfer: an improved analog reaction system of the molybdenum oxotransferases

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Modeling for the Active Site of Sulfite Oxidase: Synthesis, Characterization, and Reactivity of [MoVIO2(mnt)2]2- (mnt2- = 1,2-Dicyanoethylenedithiolate)

Das, S. K., Chaudhury, P. K., Biswas, D., & Sarkar, S. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00099a024 · Cited by 152

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

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 141

Oxomolybdenum(IV,V,VI) complexes: structures, reactivities, and criteria of detection of binuclear (.mu.-oxo)molybdenum(V) products in oxygen atom transfer systems

Craig, J. A., Harlan, E. W., Snyder, B. S., Whitener, M. A., & Holm, R. H. (1989) · Inorganic Chemistry · doi:10.1021/ic00310a015 · Cited by 136

Synthesis and Structures of Bis(dithiolene)molybdenum Complexes Related to the Active Sites of the DMSO Reductase Enzyme Family

Lim, B. S., Donahue, J. P., & Holm, R. H. (1999) · Inorganic Chemistry · doi:10.1021/ic9908672 · Cited by 134

Model for the active sites of oxo-transfer molybdoenzymes: reactivity, kinetics, and catalysis

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Comparative Kinetics of Oxo Transfer to Substrate Mediated by Bis(dithiolene)dioxomolybdenum and -tungsten Complexes

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Synthesis, Structures, and Reactivity of Bis(dithiolene)molybdenum(IV,VI) Complexes Related to the Active Sites of Molybdoenzymes

Donahue, J. P., Goldsmith, C. R., Nadiminti, U., & Holm, R. H. (1998) · Journal of the American Chemical Society · doi:10.1021/ja982914f · Cited by 128

Bis(Dithiolene)molybdenum Analogues Relevant to the DMSO Reductase Enzyme Family: Synthesis, Structures, and Oxygen Atom Transfer Reactions and Kinetics

Lim, B. S., & Holm, R. H. (2001) · Journal of the American Chemical Society · doi:10.1021/ja003546u · Cited by 127

Synthesis, Structures, and Oxo Transfer Reactivity of Bis(dithiolene)tungsten(IV,VI) Complexes Related to the Active Sites of Tungstoenzymes

Lorber, C. Y., Donahue, J. P., Goddard, C. A., Nordlander, E., & Holm, R. H. (1998) · Journal of the American Chemical Society · doi:10.1021/ja981015o · Cited by 126

Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: the 1.85 Å resolution crystal structure and its mechanistic implications 1 1Edited by I. A. Wilson

Hu, Y., Faham, S., Roy, R., Adams, M. W. W., & Rees, D. C. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2488 · Cited by 125

Structure of the Molybdenum Site of Dimethyl Sulfoxide Reductase

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Spectroscopic Evidence for a Unique Bonding Interaction in Oxo-Molybdenum Dithiolate Complexes: Implications for σ Electron Transfer Pathways in the Pyranopterin Dithiolate Centers of Enzymes

Inscore, F. E., McNaughton, R. L., Westcott, B. L., Helton, M. E., Jones, R. M., Dhawan, I. K., Enemark, J. H., & Kirk, M. L. (1999) · Inorganic Chemistry · doi:10.1021/ic981126o · Cited by 120

Modeling the Tungsten Sites of Inactive and Active Forms of Hyperthermophilic Pyrococcus furiosus Aldehyde Ferredoxin Oxidoreductase

Das, S. K., Biswas, D., Maiti, R., & Sarkar, S. (1996) · Journal of the American Chemical Society · doi:10.1021/ja9511580 · Cited by 118

Dioxomolybdenum(VI) complexes of the hydrotris(3,5-dimethyl-1-pyrazolyl)borate ligand. Synthesis and oxygen atom transfer reactions

Roberts, S. A., Young, C. G., Kipke, C. A., Cleland, W. E., YAMANOUCHI, K., Carducci, M. D., & Enemark, J. H. (1990) · Inorganic Chemistry · doi:10.1021/ic00344a007 · Cited by 115

The structure and mode of action of the cofactor of the oxomolybdoenzymes

Collison, D., Garner, C. D., & JOULE, J. A. (1996) · Chemical Society Reviews · doi:10.1039/cs9962500025 · Cited by 113

A single model displaying all the important centers and processes involved in catalysis by molybdoenzymes containing [MoVIO2]2+ active sites

Xiao, Z., Young, C. G., Enemark, J. H., & Wedd, A. G. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00049a065 · Cited by 112

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

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

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

Molybdenum(VI)-dioxo complexes with linear and tripodal tetradentate ligands: models for the molybdenum(VI/V) centers of the molybdenum hydroxylases and related enzymes. 1. Syntheses and structures

Hinshaw, C. J., Peng, G., Singh, R., Spence, J. T., Enemark, J. H., Bruck, M. A., Kristofzski, J. G., Merbs, S. L., Ortega, R. B., & Wexler, P. A. (1989) · Inorganic Chemistry · doi:10.1021/ic00324a012 · Cited by 102

Evaluation of Molybdenum−Sulfur Interactions in Molybdoenzyme Model Complexes by Gas-Phase Photoelectron Spectroscopy. The “Electronic Buffer” Effect

Westcott, B. L., Gruhn, N. E., & Enemark, J. H. (1998) · Journal of the American Chemical Society · doi:10.1021/ja972674o · Cited by 102

Reduction of nitrate to nitrite by molybdenum-mediated atom transfer: a nitrate reductase analog reaction system

Craig, J. A., & Holm, R. H. (1989) · Journal of the American Chemical Society · doi:10.1021/ja00188a026 · Cited by 101

Active Site Structures and Catalytic Mechanism ofRhodobacter sphaeroidesDimethyl Sulfoxide Reductase as Revealed by Resonance Raman Spectroscopy

Garton, S. D., Hilton, J. C., Oku, H., Crouse, B. R., Rajagopalan, K. V., & Johnson, M. K. (1997) · Journal of the American Chemical Society · doi:10.1021/ja972109l · Cited by 101

The Molybdenum Site of Sulfite Oxidase: A Comparison of Wild-Type and the Cysteine 207 to Serine Mutant Using X-ray Absorption Spectroscopy

George, G. N., Garrett, R. M., Prince, R. C., & Rajagopalan, K. V. (1996) · Journal of the American Chemical Society · doi:10.1021/ja961218h · Cited by 100

Novel Aspects of the Biochemistry of the Molybdenum Cofactor

Rajagopalan, K. V. (1991) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123102.ch5 · Cited by 96

Investigation of metal–dithiolate fold angle effects: Implications for molybdenum and tungsten enzymes

Joshi, H., Cooney, J. J. A., Inscore, F. E., Gruhn, N. E., Lichtenberger, D. L., & Enemark, J. H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0636832100 · Cited by 96

Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site 1 1Edited by P. E. Wright

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

Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 Å

Rebelo, J., Dias, J., Huber, R., Moura, J. J. G., & Romão, M. J. (2001) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750100255 · Cited by 95

X-ray Absorption Spectroscopy of Dimethyl Sulfoxide Reductase from Rhodobacter sphaeroides

George, G. N., Hilton, J. C., & Rajagopalan, K. V. (1996) · Journal of the American Chemical Society · doi:10.1021/ja953317l · Cited by 95

Syntheses, Structures, and Reactions of Binary and Tertiary Thiomolybdate Complexes Containing the (O)Mo(Sx) AND (S)Mo(Sx) Functional Groups (x = 1, 2, 4)

Coucouvanis, D. (1998) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60024-0 · Cited by 94

Studies of the reactivity of binary thio- and tertiary oxothiomolybdates toward electrophiles. Reactions with dicarbomethoxyacetylene and the synthesis and structures of the [Et4N2[MoO(L)2], anti-[Et4N]2[Mo2O2S2(L)2]], syn-[Ph4P]2[Mo2O2S2(L)2].cntdot.2DMF, Ph4P]2[Mo(L)3]DMF.cntdot.C6H6, and [Ph4P]2[Mo2S2(L)4]2CH2Cl2 complexes (L = 1,2-dicarbomethoxy-1,2-ethylenedithiolate)

Coucouvanis, D., Hadjikyriacou, A., Toupadakis, A., et al. (1991) · Inorganic Chemistry · doi:10.1021/ic00004a028 · Cited by 93

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 93

Molybdenum(V) sites in xanthine oxidase and relevant analog complexes: comparison of molybdenum-95 and sulfur-33 hyperfine coupling

Wilson, G. L., Greenwood, R. J., Pilbrow, J. R., Spence, J. T., & Wedd, A. G. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00018a014 · Cited by 91

Synthesis and Reactivity Aspects of the Bis(dithiolene) Chalcogenide Series [WIVQ(S2C2R2)2]2-(Q = O, S, Se)

Goddard, C. A., & Holm, R. H. (1999) · Inorganic Chemistry · doi:10.1021/ic9903329 · Cited by 89

Direct oxygen atom transfer in the mechanism of action of Rhodobacter sphaeroides dimethyl sulfoxide reductase

Schultz, B. E., Hille, R., & Holm, R. H. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00107a031 · Cited by 88

Oxygen atom transfer systems in which the .mu.-oxodimolybdenum(V) complex formation does not occur: syntheses, structures, and reactivities of monooxomolybdenum(IV) benzenedithiolato complexes as models of molybdenum oxidoreductases

Oku, H., Ueyama, N., Kondo, M., & Nakamura, A. (1994) · Inorganic Chemistry · doi:10.1021/ic00080a007 · Cited by 87

Oxygen Atom Transfer, Coupled Electron−Proton Transfer, and Correlated Electron−Nucleophile Transfer Reactions of Oxomolybdenum(IV) and Dioxomolybdenum(VI) Complexes

Laughlin, L. J., & Young, C. G. (1996) · Inorganic Chemistry · doi:10.1021/ic950815m · Cited by 86

Electronic spectral studies of molybdenyl complexes: implications for oxomolybdenum enzymes

Carducci, M. D., Brown, C., Solomon, E. I., & Enemark, J. H. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00105a028 · Cited by 86

Enzymatic and physiological properties of the tungsten‐substituted molybdenum TMAO reductase from Escherichia coli

Buc, J., Santini, C., Giordani, R., Czjzek, M., Wu, L., & Giordano, G. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01340.x · Cited by 85

Kinetics, mechanisms, and catalysis of oxygen atom transfer reactions of S-oxide and pyridine N-oxide substrates with molybdenum(IV,VI) complexes: relevance to molybdoenzymes

Caradonna, J. P., Reddy, P. R., & Holm, R. H. (1988) · Journal of the American Chemical Society · doi:10.1021/ja00215a022 · Cited by 83

Synthesis, characterization, and oxygen atom transfer reactions of {HB(Me2C3N2H)3}MoO{S2P(OR)2} and {HB(Me2C3N2H)3}MoO2{.eta.1-S2P(OEt)2}

Roberts, S. A., Young, C. G., Cleland, W. E., Ortega, R. B., & Enemark, J. H. (1988) · Inorganic Chemistry · doi:10.1021/ic00290a029 · Cited by 83

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 83

X-ray Absorption Spectroscopy of the Molybdenum Site of Escherichia coli Formate Dehydrogenase

George, G. N., Colangelo, C. M., Dong, J., Scott, R. A., Khangulov, S. V., Gladyshev, V. N., & Stadtman, T. C. (1998) · Journal of the American Chemical Society · doi:10.1021/ja973004l · Cited by 81

Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum

Bertram, P. A., Schmitz, R. A., Linder, D., & Thauer, R. K. (1994) · Archives of Microbiology · doi:10.1007/bf00248696 · Cited by 81

The Theoretical Transition State Structure of a Model Complex Bears a Striking Resemblance to the Active Site Structure of DMSO Reductase

Webster, C. E., & Hall, M. B. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0156486 · Cited by 80

Synthesis of oxomolybdenum bis(dithiolene) complexes related to the cofactor of the oxomolybdoenzymes †

Davies, E. S., Beddoes, R. L., Collison, D., Dinsmore, A., Docrat, A., JOULE, J. A., Wilson, C. R., & Garner, C. D. (1997) · Journal of the Chemical Society Dalton Transactions · doi:10.1039/a703682e · Cited by 79

EPR Studies of Oxo−Molybdenum(V) Complexes with Sulfur Donor Ligands: Implications for the Molybdenum Center of Sulfite Oxidase

Dhawan, I. K., & Enemark, J. H. (1996) · Inorganic Chemistry · doi:10.1021/ic9605276 · Cited by 78

Monodithiolene Molybdenum(V,VI) Complexes: A Structural Analogue of the Oxidized Active Site of the Sulfite Oxidase Enzyme Family

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Acetylene hydratase of Pelobacter acetylenicus: Molecular and spectroscopic properties of the tungsten iron–sulfur enzyme

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Kinetics of oxygen atom transfer reactions involving oxomolybdenum complexes. General treatment for reactions with intermediate oxo-bridged molybdenum(V) dimer formation

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Ligand K-Edge and Metal L-Edge X-ray Absorption Spectroscopy and Density Functional Calculations of Oxomolybdenum Complexes with Thiolate and Related Ligands: Implications for Sulfite Oxidase

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Ueyama, N., Oku, H., Kondo, M., Okamura, T., Yoshinaga, N., & Nakamura, A. (1996) · Inorganic Chemistry · doi:10.1021/ic950204u · Cited by 75

Electron Distribution in the Nonclassical Bis(dithiolene) Electron Transfer Series [M(CO)2(S2C2Me2)2]0/1-/2-(M = Mo, W): Assessment by Structural, Spectroscopic, and Density Functional Theory Results

Fomitchev, D. V., Lim, B. S., & Holm, R. H. (2001) · Inorganic Chemistry · doi:10.1021/ic001046w · Cited by 73

Kinetics of oxygen atom transfer in an analog reaction system of the molybdenum oxotransferases

Schultz, B. E., & Holm, R. H. (1993) · Inorganic Chemistry · doi:10.1021/ic00072a016 · Cited by 72

Detection, Isolation, and Characterization of Intermediates in Oxygen Atom Transfer Reactions in Molybdoenzyme Model Systems

Smith, P. D., Millar, A. J., Young, C. G., Ghosh, A. K., & Basu, P. (2000) · Journal of the American Chemical Society · doi:10.1021/ja0008362 · Cited by 72

Structural comparison of oxobis(benzene-1,2-dithiolato)molybdenum-(V) and -(IV) complexes

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A tungsten‐containing active formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei

Schmitz, R. A., RICHTER, M., LINDER, D., & Thauer, R. K. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17082.x · Cited by 71

A Density Functional Study of Oxygen Atom Transfer Reactions between Biological Oxygen Atom Donors and Molybdenum(IV) Bis(dithiolene) Complexes

Thapper, A., Deeth, R. J., & Nordlander, E. (2002) · Inorganic Chemistry · doi:10.1021/ic020385h · Cited by 70

A Catalytic Cycle Related to Molybdenum Enzymes Containing [MoVIO2]2+ Oxidized Active Sites

Xiao, Z., Bruck, M. A., Enemark, J. H., Young, C. G., & Wedd, A. G. (1996) · Inorganic Chemistry · doi:10.1021/ic961065z · Cited by 69

EXAFS analysis of xanthine oxidase complexes with alloxanthine, violapterin, and 6-pteridylaldehyde

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Aldehyde ferredoxin oxidoreductase from the hyperthermophilic archaebacterium Pyrococcus furiosus contains a tungsten oxo-thiolate center

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Reactivity of the Mo(O)(S) functional group in the [(L)Mo(O)(.mu.-S)2Mo(O)(S)]n- dimeric thiomolybdate complexes, (L = C5H5-, n = 1; S42-, n = 2) and implications regarding the function of xanthine oxidase. Synthesis and structural characterization of [(DMF)3Mo(O)(.mu.-S)2Mo(O)(S2)], [Ph4P][(C5H5)Mo(O)(.mu.-S)2Mo(O)(S2)], [Ph4P]2[(S4)Mo(O)(.mu.-S)2Mo(O)(S)] and (Et4N)4{[(S4)Mo(O)(.mu.-S)2Mo(O)(S)]2}

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Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC 27774

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

Dioxomolybdenum(VI) Complexes of Tripodal Nitrogen-Donor Ligands: Syntheses and Spectroscopic, Structural, and Electrochemical Studies, Including the Generation of EPR-Active Molybdenum(V) Species in Solution

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Tungsten Bioinorganic Chemistry: Synthesis, Structure, and Reactivity of cis-Oxothiotungsten(VI), cis-Bis(thio)tungsten(VI), and (Ene-1,2-dithiolato)tungsten(IV) Complexes

Eagle, A. A., Harben, S. M., Tiekink, E. R. T., & Young, C. G. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00100a050 · Cited by 66

Formylmethanofuran dehydrogenases from methanogenic Archaea Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron‐sulfur proteins

Bertram, P. A., Karrasch, M., Schmitz, R. A., Böcher, R., Albracht, S. P. J., & Thauer, R. K. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb18646.x · Cited by 66

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Stiefel, E. I. (1997) · Journal of the Chemical Society Dalton Transactions · doi:10.1039/a704936f · Cited by 65

Functional Analogue Reaction Systems of the DMSO Reductase Isoenzyme Family: Probable Mechanism of S-Oxide Reduction in Oxo Transfer Reactions Mediated by Bis(dithiolene)−Tungsten(IV,VI) Complexes

Sung, K.-M., & Holm, R. H. (2002) · Journal of the American Chemical Society · doi:10.1021/ja012735p · Cited by 64

Kinetics of oxygen-atom transfer reactions involving molybdenum dithiolene complexes †

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X-ray Absorption Spectroscopy of Chicken Sulfite Oxidase Crystals

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

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Structural and Functional Bis(dithiolene)-Molybdenum/Tungsten Active Site Analogues of the Dimethylsulfoxide Reductase Enzyme Family

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An oxothio-molybdenum(VI) complex stabilized by an intramolecular sulfur-sulfur interaction: implications for the active site of oxidized xanthine oxidase and related enzymes

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Mononuclear oxo thiolato compounds of molybdenum(V)

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The first mononuclear molybdenum(V) complex with a terminal sulfido ligand: dichloro[hydrotris(3,5-dimethyl-1-pyrazolyl)borato]sulfidomolybdenum

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Substitution and Oxidation Reactions of Bis(dithiolene)tungsten Complexes of Potential Relevance to Enzyme Sites

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The Unperturbed Oxo−Sulfido Functional Group cis-MoVIOS Related to That in the Xanthine Oxidase Family of Molybdoenzymes: Synthesis, Structural Characterization, and Reactivity Aspects

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Active-Site Stereochemical Control of Oxygen Atom Transfer Reactivity in Sulfite Oxidase

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Control of Oxo-Molybdenum Reduction and Ionization Potentials by Dithiolate Donors

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New Insights into the Berg−Holm Oxomolybdoenzyme Model

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Structural and Spectroscopic Characterization of a Monooxomono(dithiolene)molybdenum(V) Compound and Its Implications for the low pH Form of Sulfite Oxidase

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Tungsten-containing formate dehydrogenase from Desulfovibrio gigas: metal identification and preliminary structural data by multi-wavelength crystallography

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Oxygen Atom Transfer, Sulfur Atom Transfer, and Correlated Electron−Nucleophile Transfer Reactions of Oxo- and Thiomolybdenum(IV) Complexes: Synthesis of Oxothiomolybdenum(VI) and (Hydroxo)oxomolybdenum(V) Species

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Synthesis and Structures of Bis(dithiolene)−Tungsten(IV) Complexes Related to the Active Sites of Tungstoenzymes

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An X-ray Spectroscopic Investigation of Bis(dithiolene)molybdenum(IV,V,VI) and -tungsten(IV,V,VI) Complexes: Symmetrized Structural Representations of the Active Sites of Molybdoenzymes in the DMSO Reductase Family and of Tungstoenzymes in the AOR and F(M)DH Families

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Complexes Containing cis-[MoVO2]+ and cis-[MoVO(OH)]2+ Centers

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The mechanism of action of xanthine oxidase. The relationship between the rapid and very rapid molybdenum electron-paramagnetic-resonance signals

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Computer Modeling of the Oxygen-atom Transfer Reaction between Hydrogen Sulfite and a Molybdenum(VI) Dioxo Complex

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Synthesis and X-ray Characterization of Tetraphenylphosphonium Tetrathiocyanatodioxomolybdate(VI): A Remarkable Oxo Transfer Agent

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Model compounds for the active sites of oxo-transfer molybdoenzymes. Synthesis, structural characterization, and electrochemical properties of [NH 4 ] 2 [MoO 2 {O 2 CC(S)Ph 2 } 2 ]

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Observation of Ligand-Based Redox Chemistry at the Active Site of a Molybdenum Enzyme

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The crystal and molecular structure of tetraphenylarsonium Tetrakis(benzenethiolato)oxomolybdate(V)

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The Oxo-Gate Hypothesis and DMSO Reductase: Implications for a Psuedo-σ Bonding Interaction Involved in Enzymatic Electron Transfer

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Analogues for the Molybdenum Center of Sulfite Oxidase: Oxomolybdenum(V) Complexes with Three Thiolate Sulfur Donor Atoms

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Oxo–tungsten bis-dithiolene complexes relevant to tungsten centres in enzymes

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Toward a Total Model for the Molybdenum Hydroxylases: Synthesis, Redox, and Biomimetic Chemistry of Oxo-thio-Mo(VI) and -Mo(V) Complexes

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A broad-substrate analog reaction system of the molybdenum oxotransferases

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An Analogue System Displaying All the Important Processes of the Catalytic Cycles Involving Monooxomolybdenum(VI) and Desoxomolybdenum(IV) Centers

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A chemical approach to systematically designate the pyranopterin centers of molybdenum and tungsten enzymes and synthetic models

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Mononuclear and Binuclear Molybdenum(V) Complexes of the LigandN,N‘-Dimethyl-N,N‘-bis(2-mercaptophenyl)ethylenediamine: Geometric Isomers

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Models for the Molybdenum(VI/V) Centers of the Molybdenum Hydroxylases and Related Enzymes. Geometry, Electronic Structure, and EPR g-Tensor Predictions from ab Initio and Semiempirical Molecular Orbital Studies

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Structural Changes Induced by Catalytic Turnover at the Molybdenum Site of Arabidopsis Nitrate Reductase

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Reactions of Dimethylsulfoxide Reductase from Rhodobacter capsulatus with Dimethyl Sulfide and with Dimethyl Sulfoxide: Complexities Revealed by Conventional and Stopped-Flow Spectrophotometry

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Metal chemistry relevant to the mononuclear molybdenum and tungsten pterin enzymes

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Oxygen-17 and molybdenum-95 coupling in spectroscopic models of molybdoenzymes

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Ligand-controlled synthesis, reactivity and oxo-transfer kinetics of oxomolybdenum-(VI) and -(IV) complexes

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Association of Oxo−Molybdenum Dithiolene Complexes with a Multiamide Additive and Its Influence on the Ease of O-Atom Transfer

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Electronic Spectral Studies of Molybdenyl Complexes. 2. MCD Spectroscopy of [MoOS4]- Centers

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Atom transfer chemistry and electrochemical behavior of Mo(VI) and Mo(V) trispyrazolylborate complexes: new mononuclear and dinuclear species

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X-ray Spectroscopy of Enzyme Active Site Analogues and Related Molecules: Bis(dithiolene)molybdenum(IV) and -tungsten(IV,VI) Complexes with Variant Terminal Ligands

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Tungsten-Dependent Aldehyde Oxidoreductase: A New Family of Enzymes Containing the Pterin Cofactor

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Geometric Control of Reduction Potential in Oxomolybdenum Centers: Implications to the Serine Coordination in DMSO Reductase

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X-ray Absorption Spectroscopy of a Structural Analogue of the Oxidized Active Sites in the Sulfite Oxidase Enzyme Family and Related Molybdenum(V) Complexes

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Generation of a cis-[MoVO(OH)] center: proton- and oxygen-17 superhyperfine parameters relevant to molybdoenzymes

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CO2 fixation by [WIVO(S2C2(CN)2)2]2−: functional model for the tungsten-formate dehydrogenase ofClostridium thermoaceticum

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The cis-dioxomolybdenum(V) radical anion, [{HB(Me2C2N3)3}MoO2(SPh)]?

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Oxo/Sulfidotungstate(VI) as Precursors to WVIO2, WVIOS, and WVIS2 Complexes and WIV−Dithiolene Chelate Rings

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Dendrimer Encapsulation of [MoVOS4] Cores: Implications for the DMSO Reductase Family of Enzymes

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A mononuclear molybdenum(V) mono-oxo biphenyl-2,2′-dithiolate complex in which the metal resides within a cleft formed by the ligands and that exhibits N-H...S hydrogen bonding in the solid state

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Organometallic dioxo-, and oxo-thio- and dithio-tungsten(VI) complexes of hydrotris(3,5-dimethylpyrazolyl)borate

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Probing the Electronic Structure of [MoOS4]-Centers Using Anionic Photoelectron Spectroscopy

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Synthesis and spectroscopic characterisation of [MoO(SR) 4 ] – (R = C 6 H 5 , C 10 H 7 , 4-CH 3 C 6 H 4 , 4-ClC 6 H 4 , 3-ClC 6 H 4 , 4-FC 6 H 4 , 2,6-Cl 2 C 6 H 3 , or C 6 F 5 ) complexes and [MoO(SC 6 F 5 ) 4 ] 2–

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Synthesis, Molecular Structure, and Physical Properties of an Oxomolybdenum(IV) Complex with p-Chlorobenzenethiolate, [MoIVO(p-ClC6H4S)4]2−, as a Model of Active Sites of Reduced Molybdo-Oxidases

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Mechanism of an oxygen atom transfer reaction involving an oxo-bridged Mo(V) complex

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