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Updated: Feb 17, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Histidine tracts in human transcription factors: insight into metal ion coordination ability
Aleksandra Hecel1, Joanna Wątły2, Magdalena Rowińska-Żyrek2
1Faculty of Chemistry, University of Wroclaw, F. Joliot-Curie 14, 50-383, Wrocław, Poland. aleksandra.hecel@chem.uni.wroc.pl.
Abstract:
Consecutive histidine repeats are chosen both by nature and by molecular biologists due to their high affinity towards metal ions. Screening of the human genome showed that transcription factors are extremely rich in His tracts. In this work, we examine two of such His-rich regions from forkhead box and MAFA proteins-MB3 (contains 18 His) and MB6 (with 21 His residues), focusing on the affinity and binding modes of Cu2+ and Zn2+ towards the two His-rich regions. In the case of Zn2+ species, the availability of imidazole nitrogen donors enhances metal complex stability. Interestingly, an opposite tendency is observed for Cu2+ complexes at above physiological pH, in which amide nitrogens participate in binding.
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