The mononuclear molybdenum enzymes

Hille, Russ; Hall, James; Basu, Partha

doi:10.1021/cr400443z

Cited by 1,738Metalloenzymes and iron-sulfur proteinsMetal-Catalyzed Oxygenation MechanismsEnzyme Structure and Function

The mononuclear molybdenum enzymes

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Hille, Russ, Hall, James, Basu, Partha·2014·Chemical Reviews

DOI 10.1021/cr400443zPMC PMC4080432

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ADVERTISEMENT RETURN TO ISSUEPREVReviewThe Mononuclear Molybdenum EnzymesRuss Hille*†, James Hall†, and Partha Basu*‡View Author Information† Department of Biochemistry, University of California, Riverside, Riverside, California 92521, United States‡ Department of Chemistry and Biochemistry, Duquesne University, Pittsburgh, Pennsylvania 15282, United States*E-mail: [email protected]*E-mail: [email protected]Cite this: Chem. Rev. 2014, 114, 7, 3963–4038Publication Date (Web):January 28, 2014Publication History Received13 August 2013Published online28 January 2014Published inissue 9 April 2014https://pubs.acs.org/doi/10.1021/cr400443zhttps://doi.org/10.1021/cr400443zreview-articleACS PublicationsCopyright © 2014 American Chemical SocietyRequest reuse permissionsArticle Views10413Altmetric-Citations493LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Anions,Cluster chemistry,Molybdenum,Monomers,Peptides and proteins Get e-Alerts

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Expression and activation of bacterial nitrate reductases are tightly regulated via oxygen-dependent and nitrate-responsive mechanisms.
“Indeed, the expression and activation of bacterial nitrate reductases are tightly regulated via oxygen-dependent and nitrate-responsive mechanisms[77,256].”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [256]
NarZYW is constitutively expressed at low levels in the aerobic setting and only up-regulated in response to high nitrate concentrations, likely aiding in the transition from aerobic to anaerobic respiration.
“Conversely, NarZYW is constitutively expressed at low levels in the aerobic setting and only up-regulated in response to high nitrate concentrations, likely aiding in the transition from aerobic to anaerobic respiration [256,259,260].”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [256]
The DNRA nitrate reductase nap shares some regulatory elements with nar such as the oxygen-dependent FNR.
“Comparatively, while the DNRA nitrate reductase, nap, shares some regulatory elements with nar such as the oxygen-dependent FNR[77,256,261–264]”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [256]
NarGHI is highly oxygen-responsive, under primary transcriptional control via the oxygen sensor FNR, and appears to be the major contributor to respiratory anaerobic activity.
“The first, NarGHI, is highly oxygen-responsive, under primary transcriptional control via the oxygen sensor fumarate nitrate reductase regulator (FNR), and appears to be the major contributor to respiratory anaerobic activity[256–258].”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [256]
The respiratory nitrate reductase nar expresses two major operons, NarGHI and NarZYW.
“For instance, the respiratory nitrate reductase, nar, expresses two major operons, NarGHI and NarZYW[77,256].”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [256]

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The Metabolic Basis of Inherited Disease.
(1988) · Annals of Internal Medicine · doi:10.7326/0003-4819-108-3-503_7 · Cited by 7,807 · see citing works
Oxygen-Derived Free Radicals in Postischemic Tissue Injury
Epstein, F. H., & McCord, J. M. (1985) · New England Journal of Medicine · doi:10.1056/nejm198501173120305 · Cited by 5,399 · see citing works
X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8&nbsp;Angstrom Resolution
Peters, J. W. (1998) · Science · doi:10.1126/science.282.5395.1853 · Cited by 1,891 · see citing works
Natural engineering principles of electron tunnelling in biological oxidation–reduction
Page, C. C., Moser, C. C., Chen, X., & Dutton, P. L. (1999) · Nature · doi:10.1038/46972 · Cited by 1,866 · see citing works
Mechanism of Molybdenum Nitrogenase
Burgess, B. K., & Lowe, D. J. (1996) · Chemical Reviews · doi:10.1021/cr950055x · Cited by 1,854 · see citing works
Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas
Volbeda, A., Charon, M., Piras, C., Hatchikian, E. C., Frey, M., & Fontecilla-Camps, J. C. (1995) · Nature · doi:10.1038/373580a0 · Cited by 1,557 · see citing works
The Mononuclear Molybdenum Enzymes
Hille, R. (1996) · Chemical Reviews · doi:10.1021/cr950061t · Cited by 1,501 · see citing works
Self-citation
ABC transporters: the power to change
Rees, D. C., Johnson, E., & Lewinson, O. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2646 · Cited by 1,454 · see citing works
Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex
Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., & Jap, B. K. (1998) · Science · doi:10.1126/science.281.5373.64 · Cited by 1,253 · see citing works
Structural basis of biological nitrogen fixation
Rees, D. C., Tezcan, F. A., Haynes, C. A., Walton, M. Y., Andrade, S. L. A., Einsle, O., & Howard, J. B. (2005) · Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences · doi:10.1098/rsta.2004.1539 · Cited by 1,121 · see citing works
Metal-centered oxygen atom transfer reactions
Holm, R. H. (1987) · Chemical Reviews · doi:10.1021/cr00082a005 · Cited by 957 · see citing works
Xanthine oxidoreductase and cardiovascular disease: molecular mechanisms and pathophysiological implications
Berry, C. E., & Hare, J. M. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.055913 · Cited by 925 · see citing works
Electronic structures of active sites in copper proteins: contributions to reactivity
Solomon, E. I., Baldwin, M. J., & Lowery, M. D. (1992) · Chemical Reviews · doi:10.1021/cr00012a003 · Cited by 896 · 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
NITRATE REDUCTASE STRUCTURE, FUNCTION AND REGULATION: Bridging the Gap between Biochemistry and Physiology
Campbell, W. H. (1999) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.50.1.277 · Cited by 775 · see citing works
Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus
Sazanov, L. A., & Hinchliffe, P. (2006) · Science · doi:10.1126/science.1123809 · Cited by 763 · see citing works
The Regulation of Rat Liver Xanthine Oxidase
Stirpe, F., Corte, E. D., & Lorenzoni, E. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36428-1 · Cited by 733 · 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
The purine path to chemotherapy
Elion, G. B. (1989) · Science · doi:10.1126/science.2649979 · Cited by 687 · see citing works
Structure and mechanism of ABC transporter proteins
Hollenstein, K., Dawson, R. J. P., & Locher, K. P. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.07.003 · Cited by 672 · see citing works
The Assimilatory Nitrate-Reducing System and its Regulation
Guerrero, M. G., Vega, J. M., & Losada, M. (1981) · Annual Review of Plant Physiology · doi:10.1146/annurev.pp.32.060181.001125 · Cited by 654 · see citing works
The architecture of respiratory complex I
Efremov, R. G., Baradaran, R., & Sazanov, L. A. (2010) · Nature · doi:10.1038/nature09066 · Cited by 616 · see citing works
Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis.
Zheng, L., White, R. H., Cash, V. L., Jack, R. F., & Dean, D. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.2754 · Cited by 597 · see citing works
Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions
Berks, B. C., Ferguson, S. J., Moir, J. W. B., & Richardson, D. J. (1995) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(95)00092-5 · Cited by 596 · 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
Reversible interconversion of carbon dioxide and formate by an electroactive enzyme
Reda, T., Plugge, C. M., Abram, N. J., & Hirst, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801290105 · Cited by 561 · see citing works
Structure of a Hyperthermophilic Tungstopterin Enzyme, Aldehyde Ferredoxin Oxidoreductase
Chan, M. K., Mukund, S., Kletzin, A., Adams, M. W. W., & Rees, D. C. (1995) · Science · doi:10.1126/science.7878465 · Cited by 544 · see citing works
Atomic Structure of Ferredoxin-NADP + Reductase: Prototype for a Structurally Novel Flavoenzyme Family
Karplus, P. A., Daniels, M. J., & Herriott, J. R. (1991) · Science · doi:10.1126/science.1986412 · Cited by 536 · see citing works
The twin-arginine translocation (Tat) protein export pathway
Palmer, T., & Berks, B. C. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2814 · Cited by 536 · see citing works
Assimilatory Nitrate Reductase: Functional Properties and Regulation
Solomonson, L. P., & Barber, M. J. (1990) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.pp.41.060190.001301 · Cited by 511 · see citing works
Structure of an ABC transporter in complex with its binding protein
Hollenstein, K., Frei, D. C., & Locher, K. P. (2007) · Nature · doi:10.1038/nature05626 · Cited by 506 · 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
Genetic identification of a respiratory arsenate reductase
Saltikov, C. W., & Newman, D. K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1834303100 · Cited by 501 · see citing works
UNUSUAL COENZYMES OF METHANOGENESIS
DiMarco, A. A., Bobik, T. A., & WOLFE, R. S. (1990) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.59.070190.002035 · Cited by 496 · 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
Xanthine oxidoreductase catalyses the reduction of nitrates and nitrite to nitric oxide under hypoxic conditions
Millar, T. M., Stevens, C. R., Benjamin, N., Eisenthal, R., Harrison, R., & Blake, D. R. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00430-x · Cited by 491 · see citing works
Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli.
Zinoni, F., Birkmann, A., Stadtman, T. C., & Böck, A. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4650 · Cited by 486 · 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
Synthetic Analogues and Reaction Systems Relevant to the Molybdenum and Tungsten Oxotransferases
Enemark, J. H., Cooney, J. J. A., Wang, J., & Holm, R. H. (2003) · Chemical Reviews · doi:10.1021/cr020609d · Cited by 472 · see citing works
Microbial nitrate respiration – Genes, enzymes and environmental distribution
Kraft, B., Strous, M., & Tegetmeyer, H. E. (2011) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2010.12.025 · Cited by 465 · see citing works
The pterin molybdenum cofactors.
Rajagopalan, K. V., & Johnson, J. L. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50001-1 · Cited by 462 · see citing works
Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs
Körner, H., Sofia, H. J., & Zumft, W. G. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00066-4 · Cited by 456 · 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
Self-citation
The Arabidopsis aldehyde oxidase 3 ( AAO3 ) gene product catalyzes the final step in abscisic acid biosynthesis in leaves
Seo, M., Peeters, A. J. M., Koiwai, H., Oritani, T., Marion‐Poll, A., Zeevaart, J. A. D., Koornneef, M., Kamiya, Y., & Koshiba, T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220426197 · Cited by 440 · see citing works
Nitrate respiration in relation to facultative metabolism in enterobacteria
Stewart, V. J. (1988) · Microbiological Reviews · doi:10.1128/mr.52.2.190-232.1988 · Cited by 438 · see citing works
The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme
Corte, E. D., & Stirpe, F. (1972) · Biochemical Journal · doi:10.1042/bj1260739 · Cited by 437 · see citing works
An Extremely Potent Inhibitor of Xanthine Oxidoreductase
Okamoto, K., Eger, B. T., Nishino, T., Kondo, S., Pai, E. F., & Nishino, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208307200 · Cited by 434 · 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
Self-citation
ANTAGONISTS OF NUCLEIC ACID DERIVATIVES
Elion, G. B., Singer, S., & Hitchings, G. H. (1954) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65573-5 · Cited by 429 · see citing works
Dual requirement for gephyrin in glycine receptor clustering and molybdoenzyme activity.
Feng, G.-K., Tintrup, H., Kirsch, J., Nichol, M. C., Kuhse, J., Betz, H., & Sanes, J. (1998) · Science · doi:10.1126/science.282.5392.1321 · Cited by 425 · see citing works
Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data
Strickland, S., Palmer, G., & Massey, V. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41384-7 · Cited by 419 · see citing works
Reduction of nitrite to nitric oxide catalyzed by xanthine oxidoreductase
Godber, B. L. J., Doel, J. J., Sapkota, G. P., Blake, D. R., Stevens, C. R., Eisenthal, R., & Harrison, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7757 · Cited by 411 · see citing works
Evolution and function of ubiquitin-like protein-conjugation systems
Hochstrasser, M. (2000) · Nature Cell Biology · doi:10.1038/35019643 · Cited by 395 · see citing works
Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes
Sofia, H. J., Burland, V., Daniels, D. L., Plunkett, G., & Blattner, F. R. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.13.2576 · Cited by 392 · see citing works
The cellular and molecular origin of reactive oxygen species generation during myocardial ischemia and reperfusion
Raedschelders, K., Ansley, D. M., & Chen, D. D. Y. (2011) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.11.004 · Cited by 387 · 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
Mammalian xanthine oxidoreductase – mechanism of transition from xanthine dehydrogenase to xanthine oxidase
Nishino, T., Okamoto, K., Eger, B. T., PAI, E. F., & Nishino, T. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06489.x · Cited by 387 · see citing works
On the Mechanism of Inactivation of Xanthine Oxidase by Allopurinol and Other Pyrazolo[3,4-d]pyrimidines
Massey, V., Komai, H., Palmer, G., & Elion, G. B. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63065-0 · Cited by 380 · see citing works
Functional Modules and Structural Basis of Conformational Coupling in Mitochondrial Complex I
Hunte, C., Zickermann, V., & Brandt, U. (2010) · Science · doi:10.1126/science.1191046 · Cited by 370 · see citing works
On the Mechanism of Inactivation of Xanthine Oxidase by Cyanide
Massey, V., & Edmondson, D. E. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62575-x · Cited by 368 · see citing works
SELENIUM BIOCHEMISTRY
Stadtman, T. C. (1990) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.59.070190.000551 · Cited by 364 · 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
Tungsten in biological systems
Kletzin, A., & Adams, M. W. W. (1996) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1996.tb00226.x · Cited by 361 · 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
A comparison of the specificities of xanthine oxidase and aldehyde oxidase
Krenitsky, T. A., Neil, S. M., Elion, G. B., & Hitchings, G. H. (1972) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(72)90078-1 · Cited by 341 · see citing works
The biologically relevant oxygen atom transfer chemistry of molybdenum: from synthetic analogue systems to enzymes
Holm, R. H. (1990) · Coordination Chemistry Reviews · doi:10.1016/0010-8545(90)85010-p · Cited by 341 · 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
The Mechanism of Action of Xanthine Oxidase
Olson, J. S., Ballou, D. P., Palmer, G., & Massey, V. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42428-9 · Cited by 331 · see citing works
Nickel-Containing Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase,
Ragsdale, S. W., & Kumar, M. (1996) · Chemical Reviews · doi:10.1021/cr950058+ · Cited by 331 · see citing works
The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli.
Enoch, H. G., & Lester, R. L. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40989-7 · Cited by 322 · see citing works
Tungstoenzymes
Johnson, M. K., Rees, D. C., & Adams, M. W. W. (1996) · Chemical Reviews · doi:10.1021/cr950063d · Cited by 322 · 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
Self-citation
Identification of 22 candidate structured RNAs in bacteria using the CMfinder comparative genomics pipeline
Zasha Weinberg, A., Barrick, J. E., Yao, Z., Roth, A., Kim, J. N., Gore, J., Wang, J. X., Lee, E. R., Block, K. F., Sudarsan, N., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm487 · Cited by 312 · see citing works
New GATEWAY vectors for High Throughput Analyses of Protein–Protein Interactions by Bimolecular Fluorescence Complementation
Gehl, C., Waadt, R., Kudla, J., et al. (2009) · Molecular Plant · doi:10.1093/mp/ssp040 · Cited by 311 · see citing works
PHTHALATE DIOXYGENASE REDUCTASE: A MODULAR STRUCTURE FOR ELECTRON TRANSFER FROM PYRIDINE NUCLEOTIDES TO [2FE-2S]
Correll, C. C., Batie, C. J., Ballou, D. P., et al. (1992) · Science · doi:10.1126/science.1280857 · Cited by 298 · see citing works
The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase.
Anderson, G. L., Williams, J. W., & Hille, R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35891-5 · Cited by 297 · see citing works
Self-citation
Molecular structure of flavocytochrome b2 at 24 Å resolution
Xia, Z., & Mathews, F. S. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90240-m · Cited by 292 · see citing works
Enzyme Electrokinetics: Using Protein Film Voltammetry To Investigate Redox Enzymes and Their Mechanisms
Léger, C., Elliott, S. J., Hoke, K. R., Jeuken, L. J. C., Jones, A. K., & Armstrong, F. A. (2003) · Biochemistry · doi:10.1021/bi034789c · Cited by 289 · see citing works
Anaerobic respiration with elemental sulfur and with disulfides
Hedderich, R., Klimmek, O., Kröger, A., Dirmeier, R., Keller, M., & STETTER, K. O. (1998) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1998.tb00376.x · Cited by 289 · see citing works
The crystal structure of xanthine oxidoreductase during catalysis: Implications for reaction mechanism and enzyme inhibition
Okamoto, K., Matsumoto, K., Hille, R., Eger, B. T., Pai, E. F., & Nishino, T. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400973101 · Cited by 286 · see citing works
Self-citation
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
Hepatic Aldehyde Oxidase
Rajagopalan, K. V., Fridovich, I., & Handler, P. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60394-1 · Cited by 284 · see citing works
A Common Co-Factor for Nitrate Reductase and Xanthine Dehydrogenase which also Regulates the Synthesis of Nitrate Reductase
Pateman, J., Cove, D. J., REVER, B. M., et al. (1964) · Nature · doi:10.1038/201058a0 · Cited by 284 · see citing works
Hepatic Sulfite Oxidase
Cohen, H. J., & Fridovich, I. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62499-8 · Cited by 281 · see citing works
Characterization of the Magnitude and Kinetics of Xanthine Oxidase-catalyzed Nitrite Reduction
Li, H., Samouilov, A., Liu, X., & Zweier, J. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011648200 · Cited by 280 · see citing works
A reassessment of the FNR regulon and transcriptomic analysis of the effects of nitrate, nitrite, NarXL, and NarQP as Escherichia coli K12 adapts from aerobic to anaerobic growth
Constantinidou, C., Hobman, J. L., Griffiths, L., Patel, M. D., Penn, C. W., Cole, J. A., & Overton, T. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512312200 · Cited by 280 · see citing works
Characterization of the molybdenum cofactor of sulfite oxidase, xanthine, oxidase, and nitrate reductase. Identification of a pteridine as a structural component.
Johnson, J. L., Hainline, B. E., & Rajagopalan, K. V. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85945-8 · Cited by 279 · see citing works
Purification and properties of NADP-dependent formate dehydrogenase from Clostridium thermoaceticum, a tungsten–selenium–iron protein
Yamamoto, I., Saiki, T., Liu, S. M., & Ljungdahl, L. G. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33062-x · Cited by 276 · see citing works
Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent type to the O2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin.
Amaya, Y., Yamazaki, K., Sato, M., Noda, K., Nishino, T., & Nishino, T. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77283-9 · Cited by 275 · see citing works
Binding of nucleotides by proteins
Schulz, G. E. (1992) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(92)90178-a · Cited by 274 · see citing works
Bacterial nitrate reductases: Molecular and biological aspects of nitrate reduction
González, P. J., Correia, C., Moura, I., Brondino, C. D., & Moura, J. J. G. (2006) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2005.11.024 · Cited by 273 · see citing works
The Molybdenum Cofactor
Mendel, R. R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.455311 · Cited by 272 · see citing works
Nitric Oxide Production from Nitrite Occurs Primarily in Tissues Not in the Blood
Li, H., Cui, H., Kundu, T. K., Alzawahra, W., & Zweier, J. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801785200 · Cited by 269 · see citing works
arrA Is a Reliable Marker for As(V) Respiration
Malasarn, D., Saltikov, C. W., Campbell, K. M., Santini, J. M., Hering, J. G., & Newman, D. K. (2004) · Science · doi:10.1126/science.1102374 · Cited by 268 · see citing works
Structural and metabolic relationship between the molybdenum cofactor and urothione.
Johnson, J. L., & Rajagopalan, K. V. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.22.6856 · Cited by 266 · see citing works
Biochemical Characterization of the aba2 and aba3 Mutants in Arabidopsis thaliana
Schwartz, S. H., Léon‐Kloosterziel, K. M., Koornneef, M., & Zeevaart, J. A. D. (1997) · PLANT PHYSIOLOGY · doi:10.1104/pp.114.1.161 · Cited by 263 · see citing works
The Preparation and Properties of Deflavo Xanthine Oxidase
Komai, H., Massey, V., & Palmer, G. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91739-4 · Cited by 257 · see citing works
Olefin metathesis - a mechanistic study of high-valent Group VI catalysts
Rappé, A. K., & Goddard, W. A. (1982) · Journal of the American Chemical Society · doi:10.1021/ja00366a013 · Cited by 255 · 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
Structural Insights into Radical Generation by the Radical SAM Superfamily
Vey, J. L., & Drennan, C. L. (2011) · Chemical Reviews · doi:10.1021/cr9002616 · Cited by 254 · see citing works
Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin
Moorhead, G. B. G., Douglas, P., MORRICE, N. A., Scarabel, M., Aitken, A., & MacKintosh, C. (1996) · Current Biology · doi:10.1016/s0960-9822(02)70677-5 · Cited by 253 · see citing works
Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB–MoaD complex
Lake, M. W., Wuebbens, M. M., Rajagopalan, K. V., et al. (2001) · Nature · doi:10.1038/35104586 · Cited by 251 · 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
Metal-oxygen multiple bond lengths: a statistical study
Mayer, J. M. (1988) · Inorganic Chemistry · doi:10.1021/ic00295a006 · Cited by 245 · see citing works
Crystal structure of the S -adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans
Hänzelmann, P., & Schindelin, H. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404624101 · Cited by 243 · 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
Self-citation
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
Self-citation
Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology
Garattini, E., Mendel, R. R., Romão, M. J., Wright, R. M., & Terao, M. (2003) · Biochemical Journal · doi:10.1042/bj20030121 · Cited by 240 · see citing works
Purification and Characterization of the Selenate Reductase from Thauera selenatis
Schröder, I., Rech, S., Krafft, T., & Macy, J. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23765 · Cited by 239 · see citing works
Cotranslational insertion of selenocysteine into formate dehydrogenase from Escherichia coli directed by a UGA codon.
Zinoni, F., Birkmann, A., Leinfelder, W., & Böck, A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.10.3156 · Cited by 237 · see citing works
Tissue-Specific Localization of an Abscisic Acid Biosynthetic Enzyme, AAO3, in Arabidopsis
Koiwai, H., Nakaminami, K., Seo, M., Mitsuhashi, W., Toyomasu, T., & Koshiba, T. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.103.036970 · Cited by 236 · see citing works
Alkalilimnicola ehrlichii sp. nov., a novel, arsenite-oxidizing haloalkaliphilic gammaproteobacterium capable of chemoautotrophic or heterotrophic growth with nitrate or oxygen as the electron acceptor
Hoeft, S. E., Blum, J. S., Stolz, J. F., et al. (2007) · INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY · doi:10.1099/ijs.0.64576-0 · Cited by 236 · see citing works
Arsenic(III) Fuels Anoxygenic Photosynthesis in Hot Spring Biofilms from Mono Lake, California
Kulp, T. R., Hoeft, S. E., Asao, M., Madigan, M. T., Hollibaugh, J. T., Fisher, J. C., Stolz, J. F., Culbertson, C. W., Miller, L. G., & Oremland, R. S. (2008) · Science · doi:10.1126/science.1160799 · Cited by 235 · see citing works
Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium.
Axley, M. J., Böck, A., & Stadtman, T. C. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.19.8450 · Cited by 231 · see citing works
Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis
Krafft, T., & Macy, J. M. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2550647.x · Cited by 230 · see citing works
The prokaryotic complex iron–sulfur molybdoenzyme family
Rothery, R. A., Workun, G. J., & Weiner, J. H. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.09.002 · Cited by 224 · see citing works
Models of the Bis-Histidine-Ligated Electron-Transferring Cytochromes. Comparative Geometric and Electronic Structure of Low-Spin Ferro- and Ferrihemes
Walker, F. A. (2004) · Chemical Reviews · doi:10.1021/cr020634j · Cited by 224 · see citing works
The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives.
Johnson, J. L., Hainline, B. E., Rajagopalan, K. V., & Arison, B. H. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91027-6 · Cited by 217 · see citing works
Nitrate Assimilation by Bacteria
Lin, J. T., & Stewart, V. J. (1997) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(08)60014-4 · Cited by 216 · see citing works
The mechanism of conversion of rat liver xanthine dehydrogenase from an NAD+-dependent form (type D) to an O2-dependent form (type O)
Waud, W. R., & Rajagopalan, K. V. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90088-6 · Cited by 216 · see citing works
Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism
Kuper, J., Llamas, Á., Hecht, H., Mendel, R. R., & Schwarz, G. (2004) · Nature · doi:10.1038/nature02681 · Cited by 215 · see citing works
Microbial Sulfur Metabolism
Dahl, C., & Friedrich, C. G. (2007) · Springer eBooks · doi:10.1007/978-3-540-72682-1 · Cited by 213 · 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
Reversible light/dark modulation of spinach leaf nitrate reductase activity involves protein phosphorylation
Huber, J. L. A., Huber, S. C., Campbell, W. H., et al. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90544-7 · Cited by 211 · see citing works
The housekeeping gene xanthine oxidoreductase is necessary for milk fat droplet enveloping and secretion: gene sharing in the lactating mammary glandPreprint
Vorbach, C., Scriven, A., & Capecchi, M. R. (2002) · Genes & Development · doi:10.1101/gad.1032702 · Cited by 211 · see citing works
The Enzymology of Feedback Inhibition of Glutamine Phosphoribosylpyrophosphate Amidotransferase by Purine Ribonucleotides
Caskey, C. T., Ashton, D. M., & Wyngaarden, J. Β. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93889-5 · Cited by 210 · see citing works
Purification and properties of the NAD+-dependent (type D) and O2-dependent (type O) forms of rat liver xanthine dehydrogenase
Waud, W. R., & Rajagopalan, K. V. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90087-4 · Cited by 209 · see citing works
Comparative Studies on the Arabidopsis Aldehyde Oxidase (AAO) Gene Family Revealed a Major Role of AAO3 in ABA Biosynthesis in Seeds
Seo, M., Aoki, H., Koiwai, H., Kamiya, Y., Nambara, E., & Koshiba, T. (2004) · Plant and Cell Physiology · doi:10.1093/pcp/pch198 · Cited by 206 · see citing works
On the nature of the iron-sulfur centers in a ferredoxin from Azotobacter vinelandii. Mössbauer studies and cluster displacement experiments.
Emptage, M. H., Kent, T. A., Huynh, B. H., Rawlings, J., Orme-Johnson, W. H., & Münck, E. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85948-3 · Cited by 204 · 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 of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase.
Bachmann, M. P., Shiraishi, N., Campbell, W. H., et al. (1996) · The Plant Cell · doi:10.1105/tpc.8.3.505 · Cited by 202 · see citing works
Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component.
Axley, M. J., Grahame, D. A., & Stadtman, T. C. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44740-5 · Cited by 198 · see citing works
Evidence for a three-iron center in a ferredoxin from Desulfovibrio gigas. Mössbauer and EPR studies.
Huynh, B. H., Moura, J. J. G., Moura, I., et al. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85685-5 · Cited by 194 · see citing works
Molybdoproteomes and Evolution of Molybdenum Utilization
Zhang, Y., & Gladyshev, V. N. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.03.051 · Cited by 194 · 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
Self-citation
Sequence and nitrate regulation of the Arabidopsis thaliana mRNA encoding nitrate reductase, a metalloflavoprotein with three functional domains.
Crawford, N. M., Smith, M., Bellissimo, D. B., & Davis, R. W. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.14.5006 · Cited by 191 · see citing works
Mammalian aldehyde oxidases: genetics, evolution and biochemistry
Garattini, E., Fratelli, M., & Terao, M. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7398-y · Cited by 188 · see citing works
Crystal Structure of IscS, a Cysteine Desulfurase from Escherichia coli
Cupp‐Vickery, J. R., Urbina, H. D., & Vickery, L. E. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00690-9 · Cited by 187 · 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
Gene Sequence and the 1.8 Å Crystal Structure of the Tungsten-Containing Formate Dehydrogenase from Desulfovibrio gigas
Raaijmakers, H. C. A., Macieira, S., Dias, J. M. L., Teixeira, S. C. M., Bursakov, S. A., Huber, R., Moura, J. J. G., Moura, I., & Romão, M. J. (2002) · Structure · doi:10.1016/s0969-2126(02)00826-2 · Cited by 186 · see citing works
Ethylbenzene Dehydrogenase, a Novel Hydrocarbon-oxidizing Molybdenum/Iron-Sulfur/Heme Enzyme
Kniemeyer, O., & Heider, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101679200 · Cited by 186 · see citing works
Transfer of Thiosphaera pantotropha to Paracoccus denitrificans
Ludwig, W., Mittenhuber, G., & Friedrich, C. G. (1993) · International Journal of Systematic Bacteriology · doi:10.1099/00207713-43-2-363 · Cited by 185 · see citing works
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
Identification of a Novel Arsenite Oxidase Gene, arxA , in the Haloalkaliphilic, Arsenite-Oxidizing Bacterium Alkalilimnicola ehrlichii Strain MLHE-1
Zargar, K., Hoeft, S. E., Oremland, R. S., et al. (2010) · Journal of Bacteriology · doi:10.1128/jb.00244-10 · Cited by 181 · see citing works
Characterization of the magnitude and kinetics of xanthine oxidase-catalyzed nitrate reduction: evaluation of its role in nitrite and nitric oxide generation in anoxic tissues
Li, H., Samouilov, A., Liu, X., & Zweier, J. L. (2003) · Biochemistry · doi:10.1021/bi026385a · Cited by 180 · see citing works
The ars Detoxification System Is Advantageous but Not Required for As(V) Respiration by the Genetically Tractable Shewanella Species Strain ANA-3
Saltikov, C. W., Cifuentes, A., Venkateswaran, K. J., & Newman, D. K. (2003) · Applied and Environmental Microbiology · doi:10.1128/aem.69.5.2800-2809.2003 · Cited by 180 · see citing works
Arsenite oxidase, an ancient bioenergetic enzyme.
Lebrun, É., Brugna, M., Baymann, F., Muller, D. A. E., Lièvremont, D., Lett, M., & Nitschke, W. (2003) · Molecular biology and evolution · doi:10.1093/molbev/msg071 · Cited by 179 · see citing works
Molybdenum sites of sulfite oxidase and xanthine dehydrogenase. A comparison by EXAFS
Cramer, S. P., Wahl, R. C., & Rajagopalan, K. V. (1981) · Journal of the American Chemical Society · doi:10.1021/ja00416a005 · Cited by 177 · see citing works
Purine studies. Part I. Stability to acid and alkali. Solubility. Ionization. Comparison with pteridines
Albert, A., & Brown, D. J. (1954) · Journal of the Chemical Society (Resumed) · doi:10.1039/jr9540002060 · Cited by 176 · see citing works
Structure and function of a periplasmic nitrate reductase in Alcaligenes eutrophus H16
Siddiqui, R. A., Warnecke‐Eberz, U., Hengsberger, A., Schneider, B., Kostka, S., & Friedrich, B. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.18.5867-5876.1993 · Cited by 175 · see citing works
A thermodynamic scale for oxygen atom transfer reactions
Holm, R. H., & Donahue, J. P. (1993) · Polyhedron · doi:10.1016/s0277-5387(00)84972-4 · Cited by 174 · see citing works
DNA-binding by Ig-fold proteins.
Rudolph, M. J., & Gergen, J. P. (2001) · Nature Structural Biology · doi:10.1038/87531 · Cited by 173 · see citing works
Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation.
Schindelin, H., Rudolph, M. J., Wuebbens, M. M., et al. (2001) · Nature Structural Biology · doi:10.1038/83034 · Cited by 173 · see citing works
Crystal structure of oxidized trimethylamine N -oxide reductase from Shewanella massilia at 2.5 å resolution 1 1Edited by R. Huber
Czjzek, M., Santos, J. D., Pommier, J., Giordano, G., Méjean, V., & Haser, R. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2156 · Cited by 173 · see citing works
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
Bioinorganic Chemistry of Pterin-Containing Molybdenum and Tungsten Enzymes
Enemark, J. H., & Young, C. G. (1993) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60181-6 · Cited by 171 · see citing works
The Reaction of Xanthine Oxidase with Molecular Oxygen
Olson, J. S., Ballou, D. P., Palmer, G., & Massey, V. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42427-7 · Cited by 170 · see citing works
Nitrate reductase of Escherichia coli: Completion of the nucleotide sequence of the nar operon and reassessment of the role of the α and β subunits in iron binding and electron transfer
Blasco, F., Iobbi‐Nivol, C., Giordano, G., Chippaux, M., & Bonnefoy, V. (1989) · Molecular and General Genetics MGG · doi:10.1007/bf00331275 · Cited by 170 · see citing works
Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli
Iobbi‐Nivol, C., & Leimkühler, S. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.11.007 · Cited by 170 · see citing works
Crystal Structure of Ethylbenzene Dehydrogenase from Aromatoleum aromaticum
Kloer, D. P., Hagel, C., Heider, J., & Schulz, G. E. (2006) · Structure · doi:10.1016/j.str.2006.07.001 · Cited by 169 · see citing works
Nitrate reductases of Escherichia coli: Sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon
Blasco, F., Iobbi‐Nivol, C., Ratouchniak, J., Bonnefoy, V., & Chippaux, M. (1990) · Molecular and General Genetics MGG · doi:10.1007/bf00283030 · Cited by 168 · see citing works
Inborn errors of molybdenum metabolism: combined deficiencies of sulfite oxidase and xanthine dehydrogenase in a patient lacking the molybdenum cofactor.
Johnson, J. L., Waud, W. R., Rajagopalan, K. V., et al. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.6.3715 · Cited by 168 · see citing works
Formate-reduced E. coli formate dehydrogenase H: the reinterpretation of the crystal structure suggests a new reaction mechanism
Raaijmakers, H. C. A., & Romão, M. J. (2006) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-006-0129-2 · Cited by 167 · see citing works
Mechanism of the Conversion of Xanthine Dehydrogenase to Xanthine Oxidase
Nishino, T., Okamoto, K., Kawaguchi, Y., Hori, H., Matsumura, T., Eger, B. T., PAI, E. F., & Nishino, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501830200 · Cited by 167 · see citing works
Hepatic Sulfite Oxidase
Cohen, H. J., Fridovich, I., & Rajagopalan, K. V. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62501-3 · Cited by 166 · see citing works
Hepatic Sulfite Oxidase
Cohen, H. J., Betcher-Lange, S. L., Kessler, D. L., et al. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44588-2 · Cited by 164 · see citing works
Molecular mechanism of energy conservation in polysulfide respiration
Jormakka, M., Yokoyama, K., Yano, T., Tamakoshi, M., Akimoto, S., Shimamura, T., Curmi, P. M. G., & Iwata, S. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1434 · Cited by 164 · see citing works
Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains
Wootton, J. C., Nicolson, R. E., Cock, J. M., Walters, D. E., Burke, J. F., Doyle, W. A., & Bray, R. C. (1991) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(05)80100-8 · Cited by 164 · see citing works
Molybdenum cofactor biosynthesis and deficiency
Schwarz, G. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5269-y · Cited by 163 · see citing works
Model for the active site of oxo-transfer molybdoenzymes: synthesis, structure, and properties
Berg, J. M., & Holm, R. H. (1985) · Journal of the American Chemical Society · doi:10.1021/ja00290a029 · Cited by 163 · see citing works
A widespread riboswitch candidate that controls bacterial genes involved in molybdenum cofactor and tungsten cofactor metabolism
Regulski, E. E., Moy, R. H., Zasha Weinberg, A., Barrick, J. E., Yao, Z., Ruzzo, W. L., & Breaker, R. R. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06208.x · Cited by 162 · see citing works
Involvement of the narJ and mob gene products in distinct steps in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli
Palmer, T., Santini, C., Iobbi‐Nivol, C., Eaves, D. J., Boxer, D. H., & Giordano, G. (1996) · Molecular Microbiology · doi:10.1111/j.1365-2958.1996.tb02525.x · Cited by 162 · see citing works
Studies on the oxidative half-reaction of xanthine oxidase.
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The structure of the molybdenum cofactor. Characterization of di-(carboxamidomethyl)molybdopterin from sulfite oxidase and xanthine oxidase.
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Hänzelmann, P., & Schindelin, H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510711103 · Cited by 158 · see citing works
Purine Catabolism in Escherichia coli and Function of Xanthine Dehydrogenase in Purine Salvage
Xi, H. S., Schneider, B. L., & Reitzer, L. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.19.5332-5341.2000 · Cited by 158 · see citing works
The oxygen‐tolerant and NAD +‐dependent formate dehydrogenase from Rhodobacter capsulatus is able to catalyze the reduction of CO 2 to formate
Hartmann, T., & Leimkühler, S. (2013) · FEBS Journal · doi:10.1111/febs.12528 · Cited by 158 · 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
Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine.
Berg, B. L., Li, J., Heider, J., & Stewart, V. J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54583-x · Cited by 156 · see citing works
ISOLATION AND IDENTIFICATION OF THE XANTHINE OXIDASE FACTOR AS MOLYBDENUM
Richert, D. A., & Westerfeld, W. W. (1953) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52361-4 · Cited by 156 · see citing works
Molybdenum-mediated oxygen-atom transfer: an improved analog reaction system of the molybdenum oxotransferases
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Holm, R. H., Solomon, E. I., Majumdar, A., & Tenderholt, A. L. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.10.017 · Cited by 155 · see citing works
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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
Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli
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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
Three-dimensional structure of the iron-sulfur flavoprotein trimethylamine dehydrogenase at 2.4-A resolution.
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Flagged first, then by citations

Research works printed but not linked: 27

[1](a) Derenzo EC Heytler PG Kaleita E Arch Biochem Biophys 1954 49 242 13139688 (b) Mahler HR Mackler B Green DE Bock RM J Biol Chem 1954 210 465 13201608 (c) Nicholas DJD Nason A McElroy WD J Biol Chem 1954 207 341 13152109 (d) Cohen HJ Fridovich I Rajagopalan K J Biol Chem 1971 246 374 5100417 (e) Richert DA Westerfeld WW J Biol Chem 1953 203 915 13084661
[7](a) Magalon A Fedor JG Walburger A Weiner JH Coord Chem Rev 2011 255 1159 (b) Holm RH Solomon EI Majumdar A Tenderholt A Coord Chem Rev 2011 255 993 (c) Dobbek H Coord Chem Rev 2011 255 1104 (d) Mendel RR Schwarz G Coord Chem Rev 2011 255 1145 (e) Leimkuehler S Wuebbens MM Rajagopalan KV Coord Chem Rev 2011 255 1129 21528011 PMC3081585 (f) Metz S Thiel W Coord Chem Rev 2011 255 1085 (g) Kirk ML McNaughton RL Helton ME Prog Inorg Chem 2004 52 111 (h) Basu P Burgmayer SJN Coord Chem Rev 2011 255 1016 21607119 PMC3098623 (i) Brondino CD Rivas MG Romao MJ Moura JJG Moura I Acc Chem Res 2006 39 788 17042479 (j) Brondino CD Romao MJ Moura I Moura JJG Curr Opin Chem Biol 2006 10 109 16480912 (k) Pushie MJ George GN Coord Chem Rev 2011 255 1055 (l) Klein EL Astashkin AV Raitsimring AM Enemark JH Coord Chem Rev 2013 257 110 23440026 PMC3579671 (m) Enemark JH Cooney JJA Chem Rev 2004 104 1175 14871153 (n) Zhang Y Gladyshev VN J Mol Biol 2008 379 881 18485362 PMC2670968 (o) Leimkuhler S Wuebbens MM Rajagopalan KV Coord Chem Rev 2011 255 1129 21528011 PMC3081585 (p) Mendel RR J Biol Chem 2013 288 13165 23539623 PMC3650355 (q) Iobbi-Nivol C Leimkuhler S Biochim Biophys Acta, Bioenerg 2013 1827 1086 23201473
[66]Fisher K Llamas A Tejada-Jimenez M Schrader N Kuper J Ataya FS Galvan A Mendel RR Fernandez E Schwarz G J Biol Chem 2006 281 30186 16873364
[110]Ormejohn W Beinert H Biochem Biophys Res Commun 1969 36 337 4309781
[143](a) Ilich P Hille RJ Phys Chem B 1999 103 5406 (b) Morpeth FF George GN Bray RC Biochem J 1984 220 235 6331408 PMC1153615
[177]Olson JS Ballou DP Palmer G Massey V J Biol Chem 1974 249 4350 4367215
[179](a) Dellacor E Stirpe F Biochem J 1972 126 739 4342395 PMC1178433 (b) Stirpe F Dellacor E J Biol Chem 1969 244 3855 4308738 (c) Battelli MG Lorenzon E Stirpe F Biochem J 1973 131 191 4352904 PMC1177458 (d) Waud WR Rajagopalan KV Arch Biochem Biophys 1976 172 365 176940 (e) Nakamura M Yamazaki I J Biochem 1982 92 1279 6959993
[182](a) Harris CM Massey V Flavins and Flavoproteins 1993 1994 723 (b) Nishino T Schopfer LM Massey V J Biol Chem 1989 264 2518 2914919 (c) Schopfer LM Massey V Nishino T J Biol Chem 1988 263 13528 3166459 (d) Turner NA Doyle WA Ventom AM Bray RC Eur J Biochem 1995 232 646 7556219
[199]Neumann M Mittelstadt G Seduk F Iobbi-Nivol C Leimkuhler S J Biol Chem 2009 284 21891 19542235 PMC2755913
[214]Pauff JM Hemann CF Junemann N Leimkuhler S Hille R J Biol Chem 2007 282 12785 17327224
[235]Meyer-Klaucke W Gnida M Ferner R Gremer L Meyer O J Inorg Biochem 2001 86 339 12515558
[246](a) Holcenbe Js Stadtman ER J Biol Chem 1969 244 1194 4388026 (b) Imhoff D Andreesen JR FEMS Microbiol Lett 1979 5 155 (c) Dilworth GL Arch Biochem Biophys 1982 219 30 7181513
[252]Gladyshev VN Lecchi P BioFactors 1995 5 93 8722123
[270](a) Berg JM Holm RHJ Am Chem Soc 1984 106 3035 (b) Berg JM Holm RH J Am Chem Soc 1985 107 917 (c) Berg JM Holm RH J Am Chem Soc 1985 107 925 (d) Xiao ZG Young CG Enemark JH Wedd AG J Am Chem Soc 1992 114 9194 (e) Roberts SA Young CG Kipke CA Cleland WE Yamanouchi K Carducci MD Enemark JH Inorg Chem 1990 29 3650 (f) Basu P Kail BW Young CG Inorg Chem 2010 49 4895 20433155 PMC2897133 (g) Basu P Nemykin VN Sengar RS Inorg Chem 2009 48 6303 19485389 (h) Nemykin VN Basu P Inorg Chem 2005 44 7494 16212375
[313]Haensch R Lang C Riebeseel E Lindigkeit R Gessler A Rennenberg H Mendel RRJ Biol Chem 2006 281 6884 16407262
[315](a) Haensch R Lang C Rennenberg H Mendel RR Plant Biol (Stuttgart) 2007 9 589 17853359 (b) Brychkova G Xia Z Yang G Yesbergenova Z Zhang Z Davydov O Fluhr R Sagi M Plant J 2007 50 696 17425719
[330](a) Solomonson LP Barber M J Annu Rev Plant Physiol Plant Mol Biol 1990 41 225 (b) Campbell WH Annu Rev Plant Physiol Plant Mol Biol 1999 50 277 15012211 (c) Campbell WH Cell Mol Life Sci 2001 58 194 11289301 PMC11146515
[358](a) Kotthaus J Wahl B Havemeyer A Kotthaus J Schade D Garbe-Schoenberg D Mende R Bittner F Clement B Biochem J 2011 433 383 21029045 (b) Havemeyer A Grunewald S Wahl B Bittner F Mendel R Erdelyi P Fischer J Clement B Drug Metab Dispos 2010 38 1917 20699408
[372](a) McEwan AG Ridge JP McDevitt CA Hugenholtz P Geomicrobiol J 2002 19 3 (b) Rothery RA Workun GJ Weiner JH Biochim Biophys Acta, Biomembr 2008 1778 1897 17964535 (c) Kappler U Nouwens AS Metallomics 2013 5 325 23310928
[399]Graham N Doonan CJ Rothery RA Boroumand N Weiner JH Inorg Chem 2007 46 2 17198404
[413](a) Hedderich R Klimmek O Kroger A Dirmeier R Keller M Stetter KO FEMS Microbiol Rev 1998 22 353 (b) Dietrich W Klimmek O Eur J Biochem 2002 269 1086 11856339
[432]Plunkett G Burland V Daniels DL Blattner FR Nucleic Acids Res 1993 21 3391 8346018 PMC331436
[447](a) Tuanh NH Noriega CE Stewart V Proc Natl Acad Sci USA 2010 107 21140 21078995 PMC3000247 (b) Darwin AJ Tyson KL Busby SJW Stewart V Mol Microbiol 1997 25 583 9302020 (c) Rabin RS Collins LA Stewart V Proc Natl Acad Sci USA 1992 89 8701 1528882 PMC49988
[457](a) Majumdar A Sarkar S Coord Chem Rev 2011 255 1039 (b) Sung KM Holm RH J Am Chem Soc 2002 124 4312 11960460 (c) Sugimoto H Tsukube H Chem Soc Rev 2008 37 2609 19020675 (d) Sugimoto H Tatemoto S Suyama K Miyake H Mtei RP Itoh S Kirk ML Inorg Chem 2010 49 5368 20491454 PMC4020915 (e) Nemykin VN Davie SR Mondal S Rubie N Kirk ML Somogyi A Basu P J Am Chem Soc 2002 124 756 11817943
[474](a) Basu P Shokhirev NV Enemark JH Walker FA J Am Chem Soc 1995 117 9042 (b) Walker FA Chem Rev 2004 104 589 14871136
[494](a) Gates AJ Luque-Almagro VM Goddard AD Ferguson SJ Dolores Roldan M Richardson DJ Biochem J 2011 435 743 21348864 (b) Luque-Almagro VM Gates AJ Moreno-Vivian C Ferguson SJ Richardson DJ Roldan MD Biochem Soc Trans 2011 39 1838 22103536
[531](a) Schnell S Brune A Schink B Arch Microbiol 1991 155 511 (b) Brune A Schnell S Schink B Appl Environ Microbiol 1992 58 1861 16348719 PMC195696

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Generation of bis(dithiolene)dioxomolybdenum(vi) complexes from bis(dithiolene)monooxomolybdenum(iv) complexes by proton-coupled electron transfer in aqueous media
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Authors: Hille, R., Hall, J., & Basu, P.
Affiliations: University of California, Riverside (US)
Duquesne University (US)
Corresponding author: Hille, Russ
Basu, Partha
ORCID: Hille, Russ
Hall, James
Basu, Partha
Venue: Chemical Reviews
Publisher: American Chemical Society (ACS)
Published: 2014-01-28
Volume: 114
Issue: 7
Pages: 3963-4038
ISSN: 0009-2665 (ISSN-L)
1520-6890
DOI: 10.1021/cr400443z
PMC: PMC4080432
OpenAlex: W2045245826
Cited by: 1,738
References: 1,038
Citations by year: 2026: 41 · 2025: 55 · 2024: 64 · 2023: 65 · 2022: 63 · 2021: 79 · 2020: 72 · 2019: 65 · 2018: 70 · 2017: 69 · 2016: 77 · 2015: 72 · 2014: 80 · 2013: 52 · 2012: 60
FWCI: 3.75
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Chemical Reviews (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of General Medical Sciences (R15GM061555)
Topics: Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords: molybdenum enzymes, molybdenum clusters, molybdenum cofactor, enzyme active site, metalloproteins, metalloenzymes
MeSH terms: Aldehyde Oxidoreductases, Formate Dehydrogenases, Iron-Sulfur Proteins, Molybdenum, Nitrate Reductases, Oxidoreductases, Xanthine Oxidase, Protein Structure, Tertiary, Sulfite Oxidase, Biocatalysis

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