{ "labelLang" : "hun", "responseDate" : "2024-03-28 10:58", "content" : { "otype" : "JournalArticle", "mtid" : 31008109, "status" : "VALIDATED", "published" : true, "comment" : "Cited By :2 \n Export Date: 5 October 2020 \n CODEN: JIBID \n Correspondence Address: Kállay, C.; Department of Inorganic and Analytical Chemistry, University of DebrecenHungary; email: kallay.csilla@science.unideb.hu \n Funding details: European Commission, EU \n Funding details: Hungarian Scientific Research Fund, OTKA, NKFI-115480, NKFI-124983 \n Funding details: Magyar Tudományos Akadémia, MTA \n Funding details: European Regional Development Fund, FEDER, GINOP-2.3.2-15-2016-00008 \n Funding text 1: The authors thank the Hungarian Scientific Research Fund ( NKFI-115480 and NKFI-124983 ) for its financial support. The research was supported by the EU and co-financed by the European Regional Development Fund under the project GINOP-2.3.2-15-2016-00008 . The research was also supported by the János Bolyai Research Scholarship of the Hungarian Academy of Sciences . Appendix A\nFunding Agency and Grant Number: Hungarian Scientific Research FundOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [NKFI-115480, NKFI-124983]; EUEuropean Union (EU); European Regional Development FundEuropean Union (EU) [GINOP-2.3.2-15-2016-00008]; Janos Bolyai Research Scholarship of the Hungarian Academy of SciencesHungarian Academy of Sciences\n Funding text: The authors thank the Hungarian Scientific Research Fund (NKFI-115480 and NKFI-124983) for its financial support. The research was supported by the EU and co-financed by the European Regional Development Fund under the project GINOP-2.3.2-15-2016-00008. 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copper(II) and nickel(II) complexes, while HPLC-MS and MS/MS were used for identifying the products of copper(II) catalyzed oxidation. The copper binding ability of shorter fragments, namely the nonapeptide Ac-PHAAAGTHS-NH2 and pentapeptide Ac-PHAAA-NH2 have also been studied. The tridecapeptide is able to bind three equivalent of copper(II) ion, since the histidine residues behave as independent metal binding sites. Nevertheless, the metal binding ability of histidine residue mimicking the octarepeat domain (His85) is decreased, while the other parts of the peptide mimicking the histidines outside the octarepeat domain bind the copper ions in comparable concentration. On the other hand, this peptide is able to coordinate only two equivalents of nickel ion on the domains outside the octarepeat region. Furthermore the His96 binding site is more effective for the nickel ions. 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