HENRYK - an endless source of metal coordination surprises.
PBN-AR
Instytucja
Wydział Chemii (Uniwersytet Wrocławski)
Informacje podstawowe
Główny język publikacji
en
Czasopismo
Journal of Inorganic Biochemistry
ISSN
0162-0134
EISSN
0162-0134
Wydawca
Elsevier Science, New York
Rok publikacji
2016
Numer zeszytu
Strony od-do
258-265
Numer tomu
163
Liczba arkuszy
Słowa kluczowe
en
Histamine-like binding
Metal–peptide complexes
Thermodynamic stability
Streszczenia
Język
en
Treść
NCNThe 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.
Cechy publikacji
original-article
Inne
System-identifier
2016CH7988
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