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Structural and computational insights into the versatility of cadmium binding to proteins
Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences. Ctr Biomat Chem. (CCBG;Linnaeus Ctr Biomat Chem, BMC)ORCID iD: 0000-0001-8696-3104
2014 (English)In: Dalton Transactions, ISSN 1477-9226, E-ISSN 1477-9234, Vol. 43, no 7, p. 2878-2887Article in journal (Refereed) Published
Abstract [en]

Cadmium is a highly toxic group XII metal, similar to zinc and mercury. Unlike zinc, which is one of the most common metal cofactors in biology, cadmium is highly toxic. Many Zn2+-binding proteins can bind Cd2+-ions without significantly affecting their structures. Here, the protein data bank is analysed with regard to protein-cadmium interactions, which shows that cadmium can bind to a variety of ion binding sites in proteins. Statistical analysis of Cd2+-side chain interactions is compared with a similar analysis of other ions. This analysis reveals that with regard to amino acid side-chain preference, Cd2+ is more similar to Mn2+ than to Zn2+ or Hg2+. Finally, the interaction energies of three native metal binding proteins are calculated where Cd2+ binds instead of Zn2+, Ca2+ or Cu2+. The interaction energies are decomposed into individual components whose contributions are discussed.

Place, publisher, year, edition, pages
2014. Vol. 43, no 7, p. 2878-2887
National Category
Organic Chemistry
Research subject
Chemistry, Organic Chemistry
Identifiers
URN: urn:nbn:se:lnu:diva-32450DOI: 10.1039/c3dt52810cISI: 000330118000022Scopus ID: 2-s2.0-84892939021OAI: oai:DiVA.org:lnu-32450DiVA, id: diva2:698557
Available from: 2014-02-24 Created: 2014-02-24 Last updated: 2018-11-02Bibliographically approved

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Friedman, Ran

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