ArticleJournal of the American Chemical Society2008
Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1.
Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 73 citations in OpenAlex.
- Zinc displacement and metabolic interference: cobalt ion-mediated therapy for broad-spectrum CRKP-resistant pneumonia via inhalable microspheres.Nature communications · 2026Article
- Synergistic eradication of NDM-1Materials today. Bio · 2026Article
- The Domination of Penicillin G Degradation in Natural Surface Water: Effect of Calcium Ion and Biological Dissolved Organic Matter.Antibiotics (Basel, Switzerland) · 2025Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- A Noncanonical Metal Center Drives the Activity of the Sediminispirochaeta smaragdinae Metallo-β-lactamase SPS-1.Biochemistry · 2018Article
- A fundamental catalytic difference between zinc and manganese dependent enzymes revealed in a bacterial isatin hydrolase.Scientific reports · 2018Article
- The Continuing Challenge of Metallo-β-Lactamase Inhibition: Mechanism Matters.Trends in pharmacological sciences · 2018Review
- A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases.Nature communications · 2017Article
- Use of ferrous iron by metallo-β-lactamases.Journal of inorganic biochemistry · 2016Article
- Investigating the position of the hairpin loop in New Delhi metallo-β-lactamase, NDM-1, during catalysis and inhibitor binding.Journal of inorganic biochemistry · 2016Article
- Probing substrate binding to the metal binding sites in metallo-β-lactamase L1 during catalysis.MedChemComm · 2016Article
- Overcoming differences: The catalytic mechanism of metallo-β-lactamases.FEBS letters · 2015Review
- β-Lactam antibiotic-degrading enzymes from non-pathogenic marine organisms: a potential threat to human health.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.Biochemistry · 2014Article
- Spectroscopic and mechanistic studies of heterodimetallic forms of metallo-β-lactamase NDM-1.Journal of the American Chemical Society · 2014Article
- Biapenem inactivation by B2 metallo β-lactamases: energy landscape of the hydrolysis reaction.PloS one · 2013Article
- Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions.Nature chemical biology · 2012Article
- An unexpected similarity between antibiotic-resistant NDM-1 and beta-lactamase II from Erythrobacter litoralis.Protein & cell · 2011Article
- QM/MM studies of monozinc β-lactamase CphA suggest that the crystal structure of an enzyme-intermediate complex represents a minor pathway.Journal of the American Chemical Society · 2010Article
- Catalytic role of the metal ion in the metallo-beta-lactamase GOB.The Journal of biological chemistry · 2010Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
In an effort to probe the role of the Zn(II) sites in metallo-beta-lactamase L1, mononuclear metal ion containing and heterobimetallic analogues of the enzyme were generated and characterized using kinetic and spectroscopic studies. Mononuclear Zn(II)-containing L1, which binds Zn(II) in the consensus Zn1 site, was shown to be slightly active; however, this enzyme did not stabilize a nitrocefin-derived reaction intermediate that had been previously detected. Mononuclear Co(II)- and Fe(III)-containing L1 were essentially inactive, and NMR and EPR studies suggest that these metal ions bind to the consensus Zn2 site in L1. Heterobimetallic analogues (ZnCo and ZnFe) analogues of L1 were generated, and stopped-flow kinetic studies revealed that these enzymes rapidly hydrolyze nitrocefin and that there are large amounts of the reaction intermediate formed during the reaction. The heterobimetallic analogues were reacted with nitrocefin, and the reactions were rapidly freeze quenched. EPR studies on these samples demonstrate that Co(II) is 5-coordinate in the resting state, proceeds through a 4-coordinate species during the reaction, and is 5-coordinate in the enzyme-product complex. These studies demonstrate that the metal ion in the Zn1 site is essential for catalysis in L1 and that the metal ion in the Zn2 site is crucial for stabilization of the nitrocefin-derived reaction intermediate.
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