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Ether cross-link formation in the R2-like ligand-binding oxidase
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Uppsala University, Sweden.ORCID iD: 0000-0003-3686-3062
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0001-5574-9383
Number of Authors: 42018 (English)In: Journal of Biological Inorganic Chemistry, ISSN 0949-8257, E-ISSN 1432-1327, Vol. 23, no 6, p. 879-886Article in journal (Refereed) Published
Abstract [en]

R2-like ligand-binding oxidases contain a dinuclear metal cofactor which can consist either of two iron ions or one manganese and one iron ion, but the heterodinuclear Mn/Fe cofactor is the preferred assembly in the presence of Mn-II and Fe-II in vitro. We have previously shown that both types of cofactor are capable of catalyzing formation of a tyrosine-valine ether cross-link in the protein scaffold. Here we demonstrate that Mn/Fe centers catalyze cross-link formation more efficiently than Fe/Fe centers, indicating that the heterodinuclear cofactor is the biologically relevant one. We further explore the chemical potential of the Mn/Fe cofactor by introducing mutations at the cross-linking valine residue. We find that cross-link formation is possible also to the tertiary beta-carbon in an isoleucine, but not to the secondary beta-carbon or tertiary gamma-carbon in a leucine, nor to the primary beta-carbon of an alanine. These results illustrate that the reactivity of the cofactor is highly specific and directed.

Place, publisher, year, edition, pages
2018. Vol. 23, no 6, p. 879-886
Keywords [en]
Di-metal carboxylate protein, Ferritin, Ribonucleotide reductase, R2-like ligand-binding oxidase, X-ray crystallography
National Category
Biological Sciences Chemical Sciences
Identifiers
URN: urn:nbn:se:su:diva-159018DOI: 10.1007/s00775-018-1583-3ISI: 000439924000003PubMedID: 29946980OAI: oai:DiVA.org:su-159018DiVA, id: diva2:1246713
Available from: 2018-09-10 Created: 2018-09-10 Last updated: 2019-04-12Bibliographically approved

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Griese, Julia J.Branca, Rui M. M.Srinivas, VivekHögbom, Martin
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