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

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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

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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: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › 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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