ArticleJournal of inorganic biochemistry2014
Dilution of dipolar interactions in a spin-labeled, multimeric metalloenzyme for DEER studies.
Article in Journal of inorganic biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Synthesis and biological evaluation of novel β-lactam-metallo β-lactamase inhibitors.RSC advances · 2023Article
- Sparse Labeling PELDOR Spectroscopy on Multimeric Mechanosensitive Membrane Channels.Biophysical journal · 2017Article
- 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
- Conformational dynamics of metallo-β-lactamase CcrA during catalysis investigated by using DEER spectroscopy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
The metallo-β-lactamases (MβLs), which require one or two Zn(II) ions in their active sites for activity, hydrolyze the amide bond in β-lactam-containing antibiotics, and render the antibiotics inactive. All known MβLs contain a mobile element near their active sites, and these mobile elements have been implicated in the catalytic mechanisms of these enzymes. However little is known about the dynamics of these elements. In this study, we prepared a site-specific, double spin-labeled analog of homotetrameric MβL L1 with spin labels at positions 163 and 286 and analyzed the sample with DEER (double electron electron resonance) spectroscopy. Four unique distances were observed in the DEER distance distribution, and these distances were assigned to the desired intramolecular dipolar coupling (between spin labels at positions 163 and 286 in one subunit) and to intermolecular dipolar couplings. To rid the spin-labeled analog of L1 of the intermolecular couplings, spin-labeled L1 was "diluted" by unfolding/refolding the spin-labeled enzyme in the presence of excess wild-type L1. DEER spectra of the resulting, spin-diluted enzyme revealed a single distance corresponding to the desire intramolecular dipolar coupling.
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