ArticleJournal of bacteriology2011
Exploring the active site of the tungsten, iron-sulfur enzyme acetylene hydratase.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 50 citations in OpenAlex.
- Acetylenotrophic and DiazotrophicApplied and environmental microbiology · 2022Article
- Discovery and Characterization of the Metallopterin-Dependent Ergothioneine Synthase fromJACS Au · 2022Article
- The Effect of Pyridine-2-thiolate Ligands on the Reactivity of Tungsten Complexes toward Oxidation and Acetylene Insertion.Organometallics · 2021Article
- Epoxyqueuosine Reductase QueH in the Biosynthetic Pathway to tRNA Queuosine Is a Unique Metalloenzyme.Biochemistry · 2021Article
- Bioinspired Nucleophilic Attack on a Tungsten-Bound Acetylene: Formation of Cationic Carbyne and Alkenyl Complexes.Inorganic chemistry · 2021Article
- A Possible Primordial Acetyleno/Carboxydotrophic Core Metabolism.Life (Basel, Switzerland) · 2020Article
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- Acetylenotrophy: a hidden but ubiquitous microbial metabolism?FEMS microbiology ecology · 2018Review
- On the current role of hydratases in biocatalysis.Applied microbiology and biotechnology · 2018Review
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- Exploring the Catalytic Promiscuity of Phenolic Acid Decarboxylases: Asymmetric, 1,6-Conjugate Addition of Nucleophiles Across 4-Hydroxystyrene.Advanced synthesis & catalysis · 2017Article
- Is the tungsten(IV) complex (NEtBeilstein journal of organic chemistry · 2017Article
- Acetylene hydratase: a non-redox enzyme with tungsten and iron-sulfur centers at the active site.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Review
- Stable Carbon Isotope Fractionation during Bacterial Acetylene Fermentation: Potential for Life Detection in Hydrocarbon-Rich Volatiles of Icy Planet(oid)s.Astrobiology · 2015Article
- Degradation of acetaldehyde and its precursors by Pelobacter carbinolicus and P. acetylenicus.PloS one · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The soluble tungsten, iron-sulfur enzyme acetylene hydratase (AH) from mesophilic Pelobacter acetylenicus is a member of the dimethyl sulfoxide (DMSO) reductase family. It stands out from its class as it catalyzes a nonredox reaction, the addition of H₂O to acetylene (H-C≡C-H) to form acetaldehyde (CH₃CHO). Caught in its active W(IV) state, the high-resolution three-dimensional structure of AH offers an excellent starting point to tackle its unique chemistry and to identify catalytic amino acid residues within the active site cavity: Asp13 close to W(IV) coordinated to two molybdopterin-guanosine-dinucleotide ligands, Lys48 which couples the [4Fe-4S] cluster to the W site, and Ile142 as part of a hydrophobic ring at the end of the substrate access channel designed to accommodate the substrate acetylene. A protocol was developed to express AH in Escherichia coli and to produce active-site variants which were characterized with regard to activity and occupancy of the tungsten and iron-sulfur centers. By this means, fusion of the N-terminal chaperone binding site of the E. coli nitrate reductase NarG to the AH gene improved the yield and activity of AH and its variants significantly. Results from site-directed mutagenesis of three key residues, Asp13, Lys48, and Ile142, document their important role in catalysis of this unusual tungsten enzyme.
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