ArticleAngewandte Chemie (International ed. in English)2015
Isoprenoid Biosynthesis in Pathogenic Bacteria: Nuclear Resonance Vibrational Spectroscopy Provides Insight into the Unusual [4Fe-4S] Cluster of the E. coli LytB/IspH Protein.
Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Resonance Raman Spectroscopic Study of the Unusual [4Fe-4S]Chembiochem : a European journal of chemical biology · 2025Article
- Iron-Sulfur Cluster Enzymes of the Methylerythritol Phosphate Pathway: IspG and IspH.Biochemistry · 2025Review
- Nuclear resonant vibrational spectroscopy on Na-FeSpectroscopy letters; an international journal for rapid communication · 2025Article
- The Reductive Dehydroxylation Catalyzed by IspH, a Source of Inspiration for the Development of Novel Anti-Infectives.Molecules (Basel, Switzerland) · 2022Review
- Spectroscopic and Computational Investigations of Ligand Binding to IspH: Discovery of Non-diphosphate Inhibitors.Chembiochem : a European journal of chemical biology · 2017Article
- Structure and Function of Four Classes of the 4Fe-4S Protein, IspH.Biochemistry · 2016Article
- IspH-RPS1 and IspH-UbiA: "Rosetta Stone" Proteins.Chemical science · 2015Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 3 countries.
Funding
Abstract
The LytB/IspH protein catalyzes the last step of the methylerythritol phosphate (MEP) pathway which is used for the biosynthesis of essential terpenoids in most pathogenic bacteria. Therefore, the MEP pathway is a target for the development of new antimicrobial agents as it is essential for microorganisms, yet absent in humans. Substrate-free LytB has a special [4Fe-4S](2+) cluster with a yet unsolved structure. This motivated us to use synchrotron-based nuclear resonance vibrational spectroscopy (NRVS) in combination with quantum chemical-molecular mechanical (QM/MM) calculations to gain more insight into the structure of substrate-free LytB. The apical iron atom of the [4Fe-4S](2+) is clearly linked to three water molecules. We additionally present NRVS data of LytB bound to its natural substrate, (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate (HMBPP) and to the inhibitors (E)-4-amino-3-methylbut-2-en-1-yl diphosphate and (E)-4-mercapto-3-methylbut-2-en-1-yl diphosphate.
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Registered trials
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