دورية أكاديمية
أعرض في EDS

Gated Proton Release during Radical Transfer at the Subunit Interface of Ribonucleotide Reductase.

التفاصيل البيبلوغرافية
العنوان: Gated Proton Release during Radical Transfer at the Subunit Interface of Ribonucleotide Reductase.
المؤلفون: Cui C; Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, United States., Greene BL; Department of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, California 93106, United States., Kang G; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 20139, United States.; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 20139, United States., Drennan CL; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 20139, United States.; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 20139, United States.; Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 20139, United States.; Fellow, Bio-inspired Solar Energy Program, Canadian Institute for Advanced Research, Toronto, Ontario M5G 1M1, Canada., Stubbe J; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 20139, United States.; Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 20139, United States., Nocera DG; Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, United States.
المصدر: Journal of the American Chemical Society [J Am Chem Soc] 2021 Jan 13; Vol. 143 (1), pp. 176-183. Date of Electronic Publication: 2020 Dec 23.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 7503056 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5126 (Electronic) Linking ISSN: 00027863 NLM ISO Abbreviation: J Am Chem Soc Subsets: MEDLINE
أسماء مطبوعة: Publication: Washington, DC : American Chemical Society
Original Publication: Easton, Pa. [etc.]
مواضيع طبية MeSH: Protons*, Free Radicals/*chemistry , Ribonucleotide Reductases/*chemistry, Coordination Complexes/chemistry ; Coordination Complexes/radiation effects ; Escherichia coli/enzymology ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Glutamic Acid/chemistry ; Kinetics ; Light ; Mutagenesis, Site-Directed ; Mutation ; Oxidation-Reduction ; Rhenium/chemistry ; Rhenium/radiation effects ; Ribonucleotide Reductases/genetics ; Tyrosine/chemistry
مستخلص: The class Ia ribonucleotide reductase of Escherichia coli requires strict regulation of long-range radical transfer between two subunits, α and β, through a series of redox-active amino acids (Y 122 •[β] ↔ W 48 ?[β] ↔ Y 356 [β] ↔ Y 731 [α] ↔ Y 730 [α] ↔ C 439 [α]). Nowhere is this more precarious than at the subunit interface. Here, we show that the oxidation of Y 356 is regulated by proton release involving a specific residue, E 52 [β], which is part of a water channel at the subunit interface for rapid proton transfer to the bulk solvent. An E 52 Q variant is incapable of Y 356 oxidation via the native radical transfer pathway or non-native photochemical oxidation, following photosensitization by covalent attachment of a photo-oxidant at position 355[β]. Substitution of Y 356 for various F n Y analogues in an E 52 Q-photoβ 2 , where the side chain remains deprotonated, recovered photochemical enzymatic turnover. Transient absorption and emission data support the conclusion that Y 356 oxidation requires E 52 for proton management, suggesting its essential role in gating radical transport across the protein-protein interface.
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معلومات مُعتمدة: R01 GM029595 United States GM NIGMS NIH HHS; R01 GM047274 United States GM NIGMS NIH HHS; R35 GM126982 United States GM NIGMS NIH HHS; United States HHMI Howard Hughes Medical Institute
المشرفين على المادة: 0 (Coordination Complexes)
0 (Escherichia coli Proteins)
0 (Free Radicals)
0 (Protons)
3KX376GY7L (Glutamic Acid)
42HK56048U (Tyrosine)
7440-15-5 (Rhenium)
EC 1.17.4.- (Ribonucleotide Reductases)
تواريخ الأحداث: Date Created: 20201223 Date Completed: 20210809 Latest Revision: 20210809
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC7904477
DOI: 10.1021/jacs.0c07879
PMID: 33353307
قاعدة البيانات: MEDLINE
الوصف
تدمد:1520-5126
DOI:10.1021/jacs.0c07879