Structure and function of the unusual tungsten enzymes acetylene hydratase and class II benzoyl-coenzyme A reductase
Abstract: In biology, tungsten (W) is exclusively found in microbial enzymes bound to a bis-pyranopterin cofactor (bis-WPT). Previously known W enzymes catalyze redox oxo/hydroxyl transfer reactions by directly coordinating their substrates or products to the metal. They comprise the W-containing formate/formylmethanofuran dehydrogenases belonging to the dimethyl sulfoxide reductase (DMSOR) family and the aldehyde:ferredoxin oxidoreductase (AOR) families, which form a separate enzyme family within the Mo/W enzymes. In the last decade, initial insights into the structure and function of two unprecedented W enzymes were obtained: the acetaldehyde forming acetylene hydratase (ACH) belongs to the DMSOR and the class II benzoyl-coenzyme A (CoA) reductase (BCR) to the AOR family. The latter catalyzes the reductive dearomatization of benzoyl-CoA to a cyclic diene. Both are key enzymes in the degradation of acetylene (ACH) or aromatic compounds (BCR) in strictly anaerobic bacteria. They are unusual in either catalyzing a nonredox reaction (ACH) or a redox reaction without coordinating the substrate or product to the metal (BCR). In organic chemical synthesis, analogous reactions require totally nonphysiological conditions depending on Hg2+ (acetylene hydration) or alkali metals (benzene ring reduction). The structural insights obtained pave the way for biological or biomimetic approaches to basic reactions in organic chemistry
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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Journal of molecular microbiology and biotechnology. - 26, 1-3 (2016) , 119-137, ISSN: 1660-2412
- Keyword
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Acetylen-Hydratase
Hydratasen
- Event
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Veröffentlichung
- (where)
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Freiburg
- (who)
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Universität
- (when)
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2018
- Creator
- DOI
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10.1159/000440805
- URN
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urn:nbn:de:bsz:25-freidok-150507
- Rights
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Kein Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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25.03.2025, 1:49 PM CET
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Boll, Matthias
- Einsle, Oliver
- Ermler, Ulrich
- Kroneck, Peter M. H.
- Ullmann, G. Matthias
- Universität
Time of origin
- 2018
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Structure and Function of the Unusual Tungsten Enzymes Acetylene Hydratase and Class II Benzoyl-Coenzyme A Reductase
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Binuclear CuA formation and the influence of calcium ions on metal cluster maturation in recombinant nitrous oxide reductase from Shewanella denitrificans
On the shoulders of giants - reaching for nitrogenase
Maturation of nitrous oxide reductase by the ABC transporter complex NosDFY(L)
Structural rearrangements during copper cluster insertion into nitrous oxide reductase of Pseudomonas stutzeri
Structural analysis of the reductase component AnfH of iron-only nitrogenase from Azotobacter vinelandii
The copper chaperone NosL forms a heterometal site for Cu delivery to nitrous oxide reductase
Investigation of the protection mechanism of nitrogenase by the Shethna protein
Structural and functional characterization of the Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae and YihU of the sulfoglycolysis pathway : = Strukturelle und funktionelle Charakterisierung der Na+-translozierenden NADH:Ubichinon Oxidoreduktase aus Vibrio cholerae und YihU des Sulfoglycolysis-Stoffwechselweges
Structural Characterization of Landomycin O- and C-Glycosyltransferases
Structure and function of cytochrome c nitrite reductase
Structure and Function of the Unusual Tungsten Enzymes Acetylene Hydratase and Class II Benzoyl-Coenzyme A Reductase
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On the shoulders of giants - reaching for nitrogenase
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Structural rearrangements during copper cluster insertion into nitrous oxide reductase of Pseudomonas stutzeri
Structural analysis of the reductase component AnfH of iron-only nitrogenase from Azotobacter vinelandii
The copper chaperone NosL forms a heterometal site for Cu delivery to nitrous oxide reductase
Investigation of the protection mechanism of nitrogenase by the Shethna protein
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