Interaction of Cu2+ with His-Val-His and of Zn2+ with His-Val-Gly-Asp, two peptides surrounding metal ions in Cu,Zn-superoxide dismutase enzyme
Φόρτωση...
Ημερομηνία
Συγγραφείς
Myari, A.
Malandrinos, G.
Deligiannakis, Y.
Plakatouras, J. C.
Hadjiliadis, N.
Nagy, Z.
Sovago, I.
Τίτλος Εφημερίδας
Περιοδικό ISSN
Τίτλος τόμου
Εκδότης
Elsevier
Περίληψη
Τύπος
Είδος δημοσίευσης σε συνέδριο
Είδος περιοδικού
peer reviewed
Είδος εκπαιδευτικού υλικού
Όνομα συνεδρίου
Όνομα περιοδικού
J Inorg Biochem
Όνομα βιβλίου
Σειρά βιβλίου
Έκδοση βιβλίου
Συμπληρωματικός/δευτερεύων τίτλος
Περιγραφή
His-Val-His and His-Val-Gly-Asp are two naturally occuring peptide sequences, present at the active site of Cu,Zn-superoxide dismutase (Cu,Zn-SOD). The interactions of His-Val-His=A (copper binding site) with Cu(II) and of His-Val-Gly-Asp=B (zinc binding site) with Zn(II) have been studied by using both potentiometric and spectroscopic methods (visible, EPR, NMR). The stoichiometry, stability constants and solution structure of the complexes formed have been determined. The binding modes of the species [CuAH](2+) and [CuA](+) were characterized by histamine type of coordination. [CuA](+) is further stabilized by the formation of a macrochelate with the involvement of the imidazole of the C-terminal histidine. The existence of macrochelate results in a slight distortion of the coordination geometry providing good base for the development of enzyme models. The enhanced stability of the macrochelate suppresses the formation of bis-complexes as well as the amide deprotonation. This process, however, takes place at higher pH resulting in the formation of the 4 N- coordinated [NH2,N-,N-,N(im)] species [CuAH(2-)](-). On the other hand, in the case of the Zn(Il)-His-Val-Gly-Asp system, coordination takes place at the terminal carboxylate in species [ZnBH2](2+). Monodentate binding occurs via the N-terminal imidazole in [ZnBH](+) while histamine type of coordination is possible in [ZnB], [ZnB2H](-) and [ZnB2](2-) species. Amide deprotonation does not take place in the case of Zn2+, hydroxo-complexes are formed instead. (C) 2001 Elsevier Science B.V. All rights reserved.
Περιγραφή
Λέξεις-κλειδιά
cu2+, cu,zn-superoxide dismutase enzymes, his-val-his, his-val-gly-asp, enzyme superoxide dismutase, zinc superoxide-dismutase, base copper(ii) complex, crystal-structure, cu2zn2sod model, l-histidine, dicopper(ii), palladium(ii), ligand, platinum(ii), dipeptides
Θεματική κατηγορία
Παραπομπή
Σύνδεσμος
<Go to ISI>://000170339900003
http://ac.els-cdn.com/S0162013401002045/1-s2.0-S0162013401002045-main.pdf?_tid=38e07c2fb213d9e1d23dcc3560c170be&acdnat=1333034619_d644de7ced444adc6a944763bb924c70
http://ac.els-cdn.com/S0162013401002045/1-s2.0-S0162013401002045-main.pdf?_tid=38e07c2fb213d9e1d23dcc3560c170be&acdnat=1333034619_d644de7ced444adc6a944763bb924c70
Γλώσσα
en
Εκδίδον τμήμα/τομέας
Όνομα επιβλέποντος
Εξεταστική επιτροπή
Γενική Περιγραφή / Σχόλια
Ίδρυμα και Σχολή/Τμήμα του υποβάλλοντος
Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας