{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T14:14:49Z","timestamp":1778940889418,"version":"3.51.4"},"reference-count":36,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2022,5,26]],"date-time":"2022-05-26T00:00:00Z","timestamp":1653523200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>The systematic studies of copper(II), nickel(II) and zinc(II) ion complexes of protected multihistidine peptides containing amino acids with different side chains (Ac-SarHAH-NH2, Ac-HADH-NH2, Ac-HDAH-NH2, Ac-HXHYH-NH2 X, Y = A, F, D or K, Ac-HXHAHXH-NH2, X = F or D) have provided information about the metal ion and protein interaction and have made it possible to draw conclusions regarding general trends in the coordination of metal complexes of multihistidine peptides. The stability of the metal complexes significantly depends on the position of the histidines and amino acids, which are present in the neighbourhood of the histidine amino acids as well. The most significant effect was observed on peptides containing aspartic acid or phenylalanine. The redox parameters of complexes, however, depend on the number and position of histidines, and the other side chain donor atoms have practically no effect on the electrochemical properties of imidazole-coordinated species. However, the presence of aspartic acid side chains results in a more distorted geometry of amide-coordinated species and increases the reducibility of these complexes.<\/jats:p>","DOI":"10.3390\/molecules27113435","type":"journal-article","created":{"date-parts":[[2022,5,29]],"date-time":"2022-05-29T23:43:03Z","timestamp":1653867783000},"page":"3435","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["The Role of Side Chains in the Fine-Tuning of the Metal-Binding Ability of Multihistidine Peptides"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0009-0008-7447-4723","authenticated-orcid":false,"given":"Enik\u0151","family":"Sz\u00e9kely","sequence":"first","affiliation":[{"name":"Department of Inorganic and Analytical Chemistry, University of Debrecen, H-4032 Debrecen, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gizella","family":"Csire","sequence":"additional","affiliation":[{"name":"Department of Inorganic and Analytical Chemistry, University of Debrecen, H-4032 Debrecen, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bettina Di\u00e1na","family":"Balogh","sequence":"additional","affiliation":[{"name":"Department of Inorganic and Analytical Chemistry, University of Debrecen, H-4032 Debrecen, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1652-4506","authenticated-orcid":false,"given":"Judit Zsuzsa","family":"Erdei","sequence":"additional","affiliation":[{"name":"Department of Inorganic and Analytical Chemistry, University of Debrecen, H-4032 Debrecen, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Judit M\u00e1ria","family":"Kir\u00e1ly","sequence":"additional","affiliation":[{"name":"Department of Inorganic and Analytical Chemistry, University of Debrecen, H-4032 Debrecen, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Judit","family":"Kocsi","sequence":"additional","affiliation":[{"name":"Department of Inorganic and Analytical Chemistry, University of Debrecen, H-4032 Debrecen, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J\u00falia","family":"Pink\u00f3czy","sequence":"additional","affiliation":[{"name":"Department of Inorganic and Analytical Chemistry, University of Debrecen, H-4032 Debrecen, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0846-4689","authenticated-orcid":false,"given":"Katalin","family":"V\u00e1rnagy","sequence":"additional","affiliation":[{"name":"Department of Inorganic and Analytical Chemistry, University of Debrecen, H-4032 Debrecen, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2022,5,26]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"7326","DOI":"10.1016\/S0021-9258(19)42108-X","article-title":"Bovine erythrocyte superoxide dismutase. 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