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Updated: Feb 20, 2026

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Published on: January 17, 2020
Artificial Metalloproteins for Binding and Stabilization of a Semiquinone Radical
Nathalie Ségaud1, Ivana Drienovská1, Juan Chen1
1Stratingh Institute for Chemistry, University of Groningen , Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Abstract:
The interaction of a number of first-row transition-metal ions with a 2,2'-bipyridyl alanine (bpyA) unit incorporated into the lactococcal multidrug resistance regulator (LmrR) scaffold is reported. The composition of the active site is shown to influence binding affinities. In the case of Fe(II), we demonstrate the need of additional ligating residues, in particular those containing carboxylate groups, in the vicinity of the binding site. Moreover, stabilization of di-tert-butylsemiquinone radical (DTB-SQ) in water was achieved by binding to the designed metalloproteins, which resulted in the radical being shielded from the aqueous environment. This allowed the first characterization of the radical semiquinone in water by resonance Raman spectroscopy.
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