دورية أكاديمية
أعرض في EDS

Assembly of a heterodinuclear Mn/Fe cofactor is coupled to tyrosine-valine ether cross-link formation in the R2-like ligand-binding oxidase.

التفاصيل البيبلوغرافية
العنوان: Assembly of a heterodinuclear Mn/Fe cofactor is coupled to tyrosine-valine ether cross-link formation in the R2-like ligand-binding oxidase.
المؤلفون: Griese JJ; Department of Biochemistry and Biophysics, Stockholm University, 106 91, Stockholm, Sweden. julia.griese@icm.uu.se.; Department of Cell and Molecular Biology, Uppsala University, 751 24, Uppsala, Sweden. julia.griese@icm.uu.se., Kositzki R; Institut für Experimentalphysik, Freie Universität Berlin, 14195, Berlin, Germany., Haumann M; Institut für Experimentalphysik, Freie Universität Berlin, 14195, Berlin, Germany., Högbom M; Department of Biochemistry and Biophysics, Stockholm University, 106 91, Stockholm, Sweden. hogbom@dbb.su.se.
المصدر: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry [J Biol Inorg Chem] 2019 Mar; Vol. 24 (2), pp. 211-221. Date of Electronic Publication: 2019 Jan 28.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Springer Country of Publication: Germany NLM ID: 9616326 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1432-1327 (Electronic) Linking ISSN: 09498257 NLM ISO Abbreviation: J Biol Inorg Chem Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Berlin : Springer, c1996-
مواضيع طبية MeSH: Cross-Linking Reagents/*metabolism , Iron/*metabolism , Manganese/*metabolism , Ribonucleotide Reductases/*metabolism , Tyrosine/*metabolism , Valine/*metabolism, Cross-Linking Reagents/chemistry ; Geobacillus/enzymology ; Iron/chemistry ; Manganese/chemistry ; Point Mutation ; Ribonucleotide Reductases/chemistry ; Ribonucleotide Reductases/genetics ; Tyrosine/chemistry ; Valine/chemistry
مستخلص: R2-like ligand-binding oxidases (R2lox) assemble a heterodinuclear Mn/Fe cofactor which performs reductive dioxygen (O 2 ) activation, catalyzes formation of a tyrosine-valine ether cross-link in the protein scaffold, and binds a fatty acid in a putative substrate channel. We have previously shown that the N-terminal metal binding site 1 is unspecific for manganese or iron in the absence of O 2 , but prefers manganese in the presence of O 2 , whereas the C-terminal site 2 is specific for iron. Here, we analyze the effects of amino acid exchanges in the cofactor environment on cofactor assembly and metalation specificity using X-ray crystallography, X-ray absorption spectroscopy, and metal quantification. We find that exchange of either the cross-linking tyrosine or the valine, regardless of whether the mutation still allows cross-link formation or not, results in unspecific manganese or iron binding at site 1 both in the absence or presence of O 2 , while site 2 still prefers iron as in the wild-type. In contrast, a mutation that blocks binding of the fatty acid does not affect the metal specificity of either site under anoxic or aerobic conditions, and cross-link formation is still observed. All variants assemble a dinuclear trivalent metal cofactor in the aerobic resting state, independently of cross-link formation. These findings imply that the cross-link residues are required to achieve the preference for manganese in site 1 in the presence of O 2 . The metalation specificity, therefore, appears to be established during the redox reactions leading to cross-link formation.
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فهرسة مساهمة: Keywords: Di-metal carboxylate protein; Ferritin; R2-like ligand-binding oxidase; Ribonucleotide reductase; X-ray crystallography
المشرفين على المادة: 0 (Cross-Linking Reagents)
42HK56048U (Tyrosine)
42Z2K6ZL8P (Manganese)
E1UOL152H7 (Iron)
EC 1.17.4.- (Ribonucleotide Reductases)
EC 1.17.4.- (ribonucleotide reductase R2 subunit)
HG18B9YRS7 (Valine)
SCR Organism: Geobacillus kaustophilus
تواريخ الأحداث: Date Created: 20190129 Date Completed: 20200228 Latest Revision: 20200309
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC6399176
DOI: 10.1007/s00775-019-01639-4
PMID: 30689052
قاعدة البيانات: MEDLINE
الوصف
تدمد:1432-1327
DOI:10.1007/s00775-019-01639-4