Tungsten-containing enzymes

L'vov, N. P.; Nosikov, A. N.; Antipov, A. N.

doi:10.1023/a:1014461913945

Cited by 59Metalloenzymes and iron-sulfur proteinsEnzyme Structure and FunctionMetal-Catalyzed Oxygenation Mechanisms

Tungsten-containing enzymes

L'vov, N. P., Nosikov, A. N., Antipov, A. N.·2002·Biochemistry (Moscow)

DOI 10.1023/a:1014461913945

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Abstract

The biological importance of tungsten has been fully proved in the last decade due to isolation of a number of tungsten-containing enzymes (W-enzymes) from hyperthermophilic archaea. Tungsten was previously considered only as an antagonist of molybdenum, because the replacement of molybdenum by tungsten (due to their chemical similarity) leads to inactivation of molybdenum-containing enzymes (Mo-enzymes). In addition to the "true W-enzymes" in which tungsten cannot be replaced by molybdenum, recently some enzymes have been isolated which can use either molybdenum or tungsten in the catalytic process. This review briefly summarizes data on the participation of tungsten in catalysis by some enzymes and the structure of the active sites of W-enzymes.

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In modern extant lineages, W may fill biological roles by substituting for Mo.
“In modern extant lineages, it may also fill biological roles by substituting for Mo (e.g., Frausto da Silva and Williams, 2001;L'vov et al., 2002).”
From Trace elements at the intersection of marine biological and geochemical evolution (2016) · cites this paper as L'vov et al., 2002

Comprehensive Coordination Chemistry
Eaborn, C. (1988) · Journal of Organometallic Chemistry · doi:10.1016/0022-328x(88)83103-6 · Cited by 7,174 · see citing works
Chemistry of the elements
Greenwood, N. N., & Earnshaw, A. (1984) · Cited by 5,489 · see citing works
Encyclopedia of inorganic chemistry
(1998) · Choice Reviews Online · doi:10.5860/choice.35-5081 · Cited by 631 · 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
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
Tungstoenzymes
Johnson, M. K., Rees, D. C., & Adams, M. W. W. (1996) · Chemical Reviews · doi:10.1021/cr950063d · Cited by 322 · see citing works
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
Mukund, S., & Adams, M. W. W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98669-2 · Cited by 264 · see citing works
Structural and functional relationships of enzyme activities induced by nitrate in barley
Wray, J. L., & Filner, P. (1970) · Biochemical Journal · doi:10.1042/bj1190715 · Cited by 235 · see citing works
Metals and micronutrients. Uptake and utilization by plants
(1984) · Comparative Biochemistry and Physiology Part A Physiology · doi:10.1016/0300-9629(84)90485-7 · Cited by 189 · see citing works
Tungstate, a Molybdate Analog Inactivating Nitrate Reductase, Deregulates the Expression of the Nitrate Reductase Structural Gene
Deng, M.-D., Moureaux, T., & Caboche, M. (1989) · PLANT PHYSIOLOGY · doi:10.1104/pp.91.1.304 · Cited by 151 · see citing works
Selenium-dependent and selenium-independent formate dehydrogenases of Methanococcus vannielii. Separation of the two forms and characterization of the purified selenium-independent form.
Jones, J. B., & Stadtman, T. C. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70024-6 · Cited by 147 · see citing works
Characterization of molybdenum cofactor from Escherichia coli
Amy, N. K., & Rajagopalan, K. V. (1979) · Journal of Bacteriology · doi:10.1128/jb.140.1.114-124.1979 · Cited by 130 · see citing works
Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non‐activated carboxylic acids to aldehydes
White, H., STROBL, G., Feicht, R., & Simon, H. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb14993.x · Cited by 130 · see citing works
Characterization of a novel tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon, Thermococcus litoralis. A role for tungsten in peptide catabolism
Mukund, S., & Adams, M. W. W. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38690-9 · Cited by 114 · see citing works
The role of tungsten in the inhibition of nitrate reductase activity in spinach (spinacea oleracea L.) leaves
Notton, B. A., & Hewitt, E. J. (1971) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(71)80140-7 · Cited by 109 · see citing works
The Effect of Tungstate on Nitrate Assimilation in Higher Plant Tissues
Heimer, Y. M., Wray, J. L., & Filner, P. (1969) · PLANT PHYSIOLOGY · doi:10.1104/pp.44.8.1197 · Cited by 97 · see citing works
Effects of Molybdate, Tungstate, and Selenium Compounds on Formate Dehydrogenase and Other Enzyme Systems in Escherichia coli
Enoch, H. G., & Lester, R. L. (1972) · Journal of Bacteriology · doi:10.1128/jb.110.3.1032-1040.1972 · Cited by 94 · see citing works
A molybdenum and a tungsten isoenzyme of formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei
Schmitz, R. A., Albracht, S. P. J., & Thauer, R. K. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17376.x · Cited by 85 · see citing works
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 83 · see citing works
Purification and Molecular Characterization of the Tungsten-Containing Formaldehyde Ferredoxin Oxidoreductase from the Hyperthermophilic Archaeon Pyrococcus furiosus : the Third of a Putative Five-Member Tungstoenzyme Family
Roy, R., Mukund, S., Schut, G. J., Dunn, D. M., Weiss, R. B., & Adams, M. W. W. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.4.1171-1180.1999 · Cited by 81 · see citing works
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 79 · see citing works
Acetylene hydratase of Pelobacter acetylenicus
Meckenstock, R. U., Krieger, R., Ensign, S. H., Kroneck, P. M. H., & Schink, B. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00600.x · Cited by 77 · see citing works
Identification of molybdopterin as the organic component of the tungsten cofactor in four enzymes from hyperthermophilic Archaea.
Johnson, J. L., Rajagopalan, K. V., Mukund, S., & Adams, M. W. W. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53474-8 · Cited by 74 · see citing works
Purification and Characterization of a Tungsten-Containing Formate Dehydrogenase from Desulfovibrio gigas
Almendra, M. J., Brondino, C. D., Gavel, O. Y., Pereira, A. S., Tavares, P., Bursakov, S. A., Duarte, R. O., Caldeira, J., Moura, J. J. G., & Moura, I. (1999) · Biochemistry · doi:10.1021/bi990069n · Cited by 74 · see citing works
A selenium‐dependent and a selenium‐independent formylmethanofuran dehydrogenase and their transcriptional regulation in the hyperthermophilic Methanopyrus kandleri
Vorholt, J. A., Vaupel, M., & Thauer, R. K. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.2931653.x · Cited by 74 · see citing works
Molecular Basis of the Biological Function of Molybdenum
Johnson, J. L., Waud, W. R., Cohen, H. J., & Rajagopalan, K. V. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42327-2 · Cited by 72 · see citing works
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 · see citing works
The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum : induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme
Hochheimer, A., Hedderich, R., & Thauer, R. K. (1998) · Archives of Microbiology · doi:10.1007/s002030050658 · Cited by 69 · see citing works
Purification and Some Properties of the Tungsten-Containing Carboxylic Acid Reductase fromClostridium formicoaceticum
White, H., Feicht, R., Huber, C., Lottspeich, F., & Simon, H. (1991) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1991.372.2.999 · Cited by 68 · see citing works
The Molybdenum Formylmethanofuran Dehydrogenase Operon and the Tungsten Formylmethanofuran Dehydrogenase Operon from Methanobacterium Thermoautotrophicum
Hochheimer, A., Linder, D., Thauer, R. K., & Hedderich, R. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0156r.x · Cited by 56 · see citing works
The active sites of molybdenum- and tungsten-containing enzymes
McMaster, J., & Enemark, J. H. (1998) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(98)80061-6 · Cited by 54 · see citing works
Properties of the tungsten‐substituted molybdenum formylmethanofuran dehydrogenase from Methanobacterium wolfei
Schmitz, R. A., Albracht, S. P. J., & Thauer, R. K. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80743-z · Cited by 50 · see citing works
Effect of Tungstate on Nitrate Reduction by the Hyperthermophilic Archaeon Pyrobaculum aerophilum
Afshar, S., Kim, C., Monbouquette, H. G., & Schröder, I. (1998) · Applied and Environmental Microbiology · doi:10.1128/aem.64.8.3004-3008.1998 · Cited by 50 · see citing works
Molybdenum and vanadium do not replace tungsten in the catalytically active forms of the three tungstoenzymes in the hyperthermophilic archaeon Pyrococcus furiosus
Mukund, S., & Adams, M. W. W. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.1.163-167.1996 · Cited by 48 · see citing works
Tungsten, a biologically active metal
Ljungdahl, L. G. (1976) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(76)80193-4 · Cited by 44 · see citing works
Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: effect of tungstate and a mob mutation
Rothery, R. A., Grant, J. L., Johnson, J. L., Rajagopalan, K. V., & Weiner, J. H. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.8.2057-2063.1995 · Cited by 41 · see citing works
A chemical approach to systematically designate the pyranopterin centers of molybdenum and tungsten enzymes and synthetic models
Fischer, B., Enemark, J. H., & Basu, P. (1998) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(98)10054-5 · Cited by 41 · see citing works
Effect of Tungsten and Vanadium on the in Vitro Assembly of Assimilatory Nitrate Reductase Utilizing Neurospora Mutant nit-1
Lee, K.-Y., Erickson, R. H., Pan, S., Jones, G., May, F., & Nason, A. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42567-2 · Cited by 38 · see citing works
Purification and characterization of a benzylviologen-linked, tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas
Hensgens, C. M. H., Hagen, W. R., & Hansen, T. A. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.21.6195-6200.1995 · Cited by 37 · see citing works
In vitro reconstitution of demolybdosulfite oxidase by molybdate.
Jones, H. P., Johnson, J. L., & Rajagopalan, K. V. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40150-5 · Cited by 32 · see citing works
Kinetic Studies of a Soluble αβ Complex of Nitrate Reductase A from Escherichia Coli
Buc, J., Santini, C., Blasco, F., Giordani, R., Cárdenas, M. L., Chippaux, M., Cornish-Bowden, A. J., & Giordano, G. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.766_a.x · Cited by 29 · see citing works
Novel growth characteristics and high rates of nitrate reduction of an Escherichia coli strain, LCB2048, that expresses only a periplasmic nitrate reductase
POTTER, L. C., Millington, P. D., Thomas, G. H., Rothery, R. A., Giordano, G., & Cole, J. A. (2000) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2000.tb09039.x · Cited by 19 · see citing works
Micronutrients and Nitrate Reductase
Notton, B. A. (1983) · Elsevier eBooks · doi:10.1016/b978-0-12-589580-4.50020-1 · Cited by 19 · see citing works
Transition metal requirement to express high level NAD+-dependent formate dehydrogenase from a serine-type methylotrophic bacterium
GÃrio, F. M., Marcos, J. C., & Amaral-Collaço, M. T. (1992) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1992.tb05456.x · Cited by 16 · see citing works
Activation of nit-1 nitrate reductase by W-formate dehydrogenase
Deaton, J. C., Solomon, E. I., Durfor, C. N., Wetherbee, P. J., Burgess, B. K., & Jacobs, D. B. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)90782-4 · Cited by 11 · see citing works
Molybdenum and iron as functional constituents of the enzymes of the nitrate-reducing system of Azotobacter chroococcum
Guerrero, M. G., & Vega, J. M. (1975) · Archives of Microbiology · doi:10.1007/bf00428351 · Cited by 9 · see citing works
The Effect of the Simultaneous Addition of Molybdenum and Tungsten to the Culture Medium on the Formate Dehydrogenase Activity from Methylobacterium sp. RXM
Gírio, F. M., Roseiro, J. C., & Silva, A. I. (1998) · Current Microbiology · doi:10.1007/s002849900319 · Cited by 8 · see citing works
Stimulation of nitrate reductase activity of the salt-tolerant yeast Rhodotorula glutinis by tungsten in the presence of molybdenum.
Nosikov, A. N., Ev, C., Li, G., Zvyagilskaya, R. A., & Np, L. (2000) · PubMed · Cited by 5 · see citing works

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Trace elements at the intersection of marine biological and geochemical evolution
Robbins, L. J., Lalonde, S. V., Planavsky, N. J., Partin, C. A., Reinhard, C. T., Kendall, B., Scott, C., Hardisty, D. S., Gill, B. C., Alessi, D. S., et al. (2016) · Earth-Science Reviews · doi:10.1016/j.earscirev.2016.10.013 · Cited by 227 · see citing works
Biogeochemical signatures through time as inferred from whole microbial genomes
Zerkle, A. L. (2005) · American Journal of Science · doi:10.2475/ajs.305.6-8.467 · Cited by 223 · see citing works
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Moore, E. K., Jelen, B. I., Giovannelli, D., Raanan, H., & Falkowski, P. G. (2017) · Nature Geoscience · doi:10.1038/ngeo3006 · Cited by 197 · see citing works
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Valdez, C. E., Smith, Q. A., Nechay, M. R., & Alexandrova, A. N. (2014) · Accounts of Chemical Research · doi:10.1021/ar500227u · Cited by 179 · see citing works
Bioethanol production from biomass: carbohydrate vs syngas fermentation
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Thiosulfoxide (sulfane) sulfur: new chemistry and new regulatory roles in biology
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Comparative Genomics of Trace Elements: Emerging Dynamic View of Trace Element Utilization and Function
Zhang, Y., & Gladyshev, V. N. (2009) · Chemical Reviews · doi:10.1021/cr800557s · Cited by 143 · see citing works
Mechanism of tungsten-dependent acetylene hydratase from quantum chemical calculations
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Tungsten, the Surprisingly Positively Acting Heavy Metal Element for Prokaryotes
Andreesen, J. R., & Makdessi, K. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1419.003 · Cited by 94 · see citing works
Effect of tungstate on acetate and ethanol production by the electrosynthetic bacterium Sporomusa ovata
Ammam, F., Tremblay, P., Lizak, D. M., & Zhang, T. (2016) · Biotechnology for Biofuels · doi:10.1186/s13068-016-0576-0 · Cited by 88 · see citing works
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van der Voet, G. B., Todorov, T. I., Centeno, J. A., Jonas, W. B., Ives, J. A., & Mullick, F. G. (2007) · Military Medicine · doi:10.7205/milmed.172.9.1002 · Cited by 73 · see citing works
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Ancient biosphere: The origin, trends and events
Fedonkin, M. A. (2008) · Rossijskij žurnal nauk o zemle/Russian journal of earth sciences · doi:10.2205/2007es000252 · Cited by 8 · see citing works
Ionic strength dependence of stability constants, complexation of W(VI) with iminodiacetic acid
Majlesi, K., Zare, K., & Najafi, F. (2007) · Russian Journal of Inorganic Chemistry · doi:10.1134/s0036023607080232 · Cited by 7 · see citing works
Synthesis, characterization, and DNA binding of the biologically relevant novel cationic molybdenum(VI)–glutathione complex [Mo(GS)(Cl)(H2O)]Cl2
Selim, M., Saha, A., & Mukherjea, K. K. (2011) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/s00706-011-0601-8 · Cited by 6 · see citing works
Solid phase synthesis and structural characterization of an oxo-molybdenum(V) porphyrin: triplet state ESR spectrum of μ-oxo bridged molybdenum(V) dimer
Nandi, G., & Sarkar, S. (2014) · Journal of Porphyrins and Phthalocyanines · doi:10.1142/s1088424613501277 · Cited by 6 · see citing works
Effect of tungstate on pea root growth and protein tyrosine phosphorylation
Gazizova, N., Petrova, N. V., & Karimova, F. G. (2013) · Russian Journal of Plant Physiology · doi:10.1134/s1021443713050051 · Cited by 5 · see citing works
Relativistic effect behind the molybdenum vs . tungsten selectivity in enzymes
Das, U., Das, A., & Das, A. K. (2025) · Dalton Transactions · doi:10.1039/d5dt00001g · Cited by 5 · see citing works
A sensitive kinetic spectrophotometric determination of traces of tungsten in solution based on its inhibitory effect on the decolorization reaction of potassium permanganate
Petković, B. B., Micić, R. J., & Simonović, R. M. (2016) · University thought - Publication in Natural Sciences · doi:10.5937/univtho6-10437 · Cited by 4 · see citing works
Identification of Key Organisms, Genes and Pathways in Benzene-degrading Methanogenic Cultures
Devine, C. E. (2013) · TSpace (University of Toronto) · Cited by 5 · see citing works
Metalloproteins
Degtyarenko, K. N. (2005) · Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics · doi:10.1002/047001153x.g306204 · Cited by 4 · see citing works
Isolation, Purification, and Characterization of Nitrate Reductase from a Salt-Tolerant Rhodotorula glutinis Yeast Strain Grown in the Presence of Tungsten
Morozkina, E. V., Nosikov, A. N., Zvyagilskaya, R. A., & L'vov, N. P. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0188-y · Cited by 3 · see citing works
A QM/MM investigation of the catalytic mechanism of acetylene hydratase: insights into engineering a more effective enzyme
Zhang, W., & Bushnell, E. A. C. (2020) · Canadian Journal of Chemistry · doi:10.1139/cjc-2020-0322 · Cited by 1 · see citing works
Comparison of the application of Debye-Huckel and specific ion interaction theories for the complexation of tungsten(VI) with ethylenediaminediacetic acid
Majlesi, K., Zare, K., Rezaienejad, S., & Nemati, F. (2009) · Russian Journal of Inorganic Chemistry · doi:10.1134/s0036023609050209 · Cited by 1 · see citing works
Early Eukaryotization of Life: Environmental Driving Forces of Evolution
Fedonkin, M. A. (2008) · Hokkaido University Collection of Scholarly and Academic Papers (Hokkaido University) · Cited by 1 · see citing works
First Steps in Evolution of Prokaryotes: Anaerobic Chemotypes Four to Three Billion Years Ago
Williams, R. J., & da Silva, J. J. R. F. (2006) · Elsevier eBooks · doi:10.1016/b978-044452115-6/50048-8
INTERACTION OF OBLIGATE ANAEROBIC DESTROYER OF SOLID ORGANIC WASTE Clostridium butyricum GMP1 WITH SOLUBLE COMPOUNDS OF TOXIC METALS Cr(VI), Mo(VI) AND W(VI)
Hovorukha, V. (2020) · Biotechnologia Acta · doi:10.15407/biotech13.05.073
References
(2010) · Calcium binding proteins · doi:10.1002/9780470872390.refs
References
(2009) · Wiley eBooks · doi:10.1002/9780470447758.refs
Introduction to metalloenzymes: From bench to bedside
Donald, W. A., & Supuran, C. T. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-823974-2.00038-3
Biomaterials
Edirisinghe, M. J., Gültekinoğlu, M., & Ahmed, J. (2024) · Institute of Physics eBooks · doi:10.1088/978-0-7503-5187-4
Metal binding site alignment enables network-driven discovery of recurrent geometries across sequence-divergent proteins and drug off-targets
Simensen, V., & Almaas, E. (2026) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1014636

Authors: L'vov, N. P., Nosikov, A. N., & Antipov, A. N.
Affiliations: Russian Academy of Sciences (RU)
Corresponding author: L'vov, N. P.
ORCID: Antipov, A. N.
Venue: Biochemistry (Moscow)
Publisher: Springer Science and Business Media LLC
Published: 2002-02
Volume: 67
Issue: 2
Pages: 196-200
ISSN: 0006-2979 (ISSN-L)
1608-3040
DOI: 10.1023/a:1014461913945
OpenAlex: W1536311713
Cited by: 59
References: 50
Citations by year: 2026: 1 · 2025: 2 · 2024: 3 · 2023: 4 · 2020: 2 · 2019: 4 · 2018: 3 · 2017: 2 · 2016: 5 · 2015: 2 · 2014: 3 · 2013: 3 · 2012: 2
FWCI: 1.30
Type: journal article
Language: en
Open access: closed
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Biochemistry (Moscow) (publishedVersion)
PubMed (publishedVersion)
Topics: Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords: tungsten, hyperthermophilic archaea, molybdenum-containing enzymes, enzyme catalysis, active site structure, metalloenzymes
MeSH terms: Bacteria, Bacterial Proteins, Binding Sites, Enzymes, Models, Molecular, Molybdenum, Tungsten

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