ArticleInorganic chemistry2019
A Biochemical Nickel(I) State Supports Nucleophilic Alkyl Addition: A Roadmap for Methyl Reactivity in Acetyl Coenzyme A Synthase.
Article in Inorganic chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- A protein-based model of carbon monoxide dehydrogenase exhibits tunable covalency across cluster oxidation and ligand-bound states.Chemical science · 2026Article
- The mechanism of acetyl-CoA synthase through the lens of a nickel model system.Nature communications · 2025Article
- Mixed Valence {NiJournal of the American Chemical Society · 2024Article
- Electronic isomerism in a heterometallic nickel-iron-sulfur cluster models substrate binding and cyanide inhibition of carbon monoxide dehydrogenase.Chemical science · 2024Article
- Characterization of Methyl- and Acetyl-Ni Intermediates in Acetyl CoA Synthase Formed during Anaerobic COJournal of the American Chemical Society · 2023Article
- A De Novo Designed Trimeric Metalloprotein as a NiInternational journal of molecular sciences · 2023Article
- Structural Insights into Microbial One-Carbon Metabolic Enzymes Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenases and Acetyl-CoA Synthases.Biochemistry · 2022Review
- Thioester synthesis by a designed nickel enzyme models prebiotic energy conversion.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Repurposing metalloproteins as mimics of natural metalloenzymes for small-molecule activation.Journal of inorganic biochemistry · 2021Review
- De novo biosynthesis of a nonnatural cobalt porphyrin cofactor inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase.ACS catalysis · 2020Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Nickel-containing enzymes such as methyl coenzyme M reductase (MCR) and carbon monoxide dehydrogenase/acetyl coenzyme A synthase (CODH/ACS) play a critical role in global energy conversion reactions, with significant contributions to carbon-centered processes. These enzymes are implied to cycle through a series of nickel-based organometallic intermediates during catalysis, though identification of these intermediates remains challenging. In this work, we have developed and characterized a nickel-containing metalloprotein that models the methyl-bound organometallic intermediates proposed in the native enzymes. Using a nickel(I)-substituted azurin mutant, we demonstrate that alkyl binding occurs via nucleophilic addition of methyl iodide as a methyl donor. The paramagnetic Ni
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