HENRYK — An endless source of metal coordination surprises

July 28, 2017


HENRYK — An endless source of metal coordination surprises


Paulina Kolkowska, Aleksandra Hecel, Dorota Kędzierska, Małgorzata Ostrowska, Paulina K. Walencik, Joanna Wątły, Karolina Zdyb, Marta Spodzieja, Sylwia Rodziewicz-Motowidło, Sławomir Potocki, Marek Łuczkowski, Elżbieta Gumienna-Kontecka, Magdalena Rowińska-Żyrek




Journal of Inorganic Biochemistry


The basic knowledge about biological inorganic chemistry, thermodynamics and metal binding sites of metalloproteins is crucial for the understanding of their metal binding–structure–function relationship. Metal–peptide complexes are useful and commonly used models of metal–enzyme active sites, among which copper and zinc models are one of the most extensively studied. HENRYK is a peptide sequence present in numerous proteins, and serves as a potentially tempting binding site for Cu2+ and Zn2+. Maybe more importantly, HENRYK also happens to be the first name of our group leader. The results of this work, which, at the first glance, might seem to be a ‘chemical scrabble’, went far beyond our expectations and surprised us with a novel, uncommon behavior of a Cu2+ complex with a peptide with a histidine in position one. At low pH, the binding is a typical histamine-like coordination, but with the increase of pH, the imidazole nitrogen is moved to the axial position and replaced with an amide; at basic pH, the binding mode is a {NH2, 3N−} one in the equatorial plane. It is important to note, that no dimeric species are formed in between. Such binding is thermodynamically much more stable than a simple complex with histamine, and quite comparable to complexes with several possible imidazole anchoring sites.




Circular dichroism, Ligand binding, Coordination chemistry, Biochemistry, Inorganic chemistry