دورية أكاديمية
أعرض في EDS

19 F Electron-Nuclear Double Resonance Reveals Interaction between Redox-Active Tyrosines across the α/β Interface of E. coli Ribonucleotide Reductase.

التفاصيل البيبلوغرافية
العنوان: 19 F Electron-Nuclear Double Resonance Reveals Interaction between Redox-Active Tyrosines across the α/β Interface of E. coli Ribonucleotide Reductase.
المؤلفون: Meyer A; Research group ESR spectroscopy, Max Planck Institute for Multidisciplinary Sciences, 37077 Göttingen, Germany., Kehl A; Research group ESR spectroscopy, Max Planck Institute for Multidisciplinary Sciences, 37077 Göttingen, Germany., Cui C; Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, United States., Reichardt FAK; Research group ESR spectroscopy, Max Planck Institute for Multidisciplinary Sciences, 37077 Göttingen, Germany., Hecker F; Research group ESR spectroscopy, Max Planck Institute for Multidisciplinary Sciences, 37077 Göttingen, Germany., Funk LM; Department of structural dynamics, Max Planck Institute for Multidisciplinary Sciences, 37077 Göttingen, Germany.; Department of Molecular Enzymology, Georg-August University, 37077 Göttingen, Germany., Ghosh MK; Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, United States., Pan KT; Research group bioanalytical mass spectrometry, Max Planck Institute for Multidisciplinary Sciences, 37077 Göttingen, Germany.; Bioanalytics, University Medical Center, 37075 Göttingen, Germany., Urlaub H; Research group bioanalytical mass spectrometry, Max Planck Institute for Multidisciplinary Sciences, 37077 Göttingen, Germany.; Bioanalytics, University Medical Center, 37075 Göttingen, Germany., Tittmann K; Department of structural dynamics, Max Planck Institute for Multidisciplinary Sciences, 37077 Göttingen, Germany.; Department of Molecular Enzymology, Georg-August University, 37077 Göttingen, Germany., Stubbe J; Department of Chemistry and Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 20139, United States., Bennati M; Research group ESR spectroscopy, Max Planck Institute for Multidisciplinary Sciences, 37077 Göttingen, Germany.; Department of Chemistry, Georg-August University, 37077 Göttingen, Germany.
المصدر: Journal of the American Chemical Society [J Am Chem Soc] 2022 Jun 29; Vol. 144 (25), pp. 11270-11282. Date of Electronic Publication: 2022 Jun 02.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't; Research Support, N.I.H., Extramural
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: Ribonucleotide Reductases*/chemistry, Electron Spin Resonance Spectroscopy ; Electrons ; Escherichia coli/metabolism ; Fluorine ; Models, Molecular ; Oxidation-Reduction ; Protons ; Tyrosine/chemistry
مستخلص: Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides to deoxyribonucleotides, thereby playing a key role in DNA replication and repair. Escherichia coli class Ia RNR is an α 2 β 2 enzyme complex that uses a reversible multistep radical transfer (RT) over 32 Å across its two subunits, α and β, to initiate, using its metallo-cofactor in β 2 , nucleotide reduction in α 2 . Each step is proposed to involve a distinct proton-coupled electron-transfer (PCET) process. An unresolved step is the RT involving Y 356 (β) and Y 731 (α) across the α/β interface. Using 2,3,5-F 3 Y 122 -β 2 with 3,5-F 2 Y 731 -α 2 , GDP (substrate) and TTP (allosteric effector), a Y 356 • intermediate was trapped and its identity was verified by 263 GHz electron paramagnetic resonance (EPR) and 34 GHz pulse electron-electron double resonance spectroscopies. 94 GHz 19 F electron-nuclear double resonance spectroscopy allowed measuring the interspin distances between Y 356 • and the 19 F nuclei of 3,5-F 2 Y 731 in this RNR mutant. Similar experiments with the double mutant E 52 Q/F 3 Y 122 -β 2 were carried out for comparison to the recently published cryo-EM structure of a holo RNR complex. For both mutant combinations, the distance measurements reveal two conformations of 3,5-F 2 Y 731 . Remarkably, one conformation is consistent with 3,5-F 2 Y 731 within the H-bond distance to Y 356 • , whereas the second one is consistent with the conformation observed in the cryo-EM structure. The observations unexpectedly suggest the possibility of a colinear PCET, in which electron and proton are transferred from the same donor to the same acceptor between Y 356 and Y 731 . The results highlight the important role of state-of-the-art EPR spectroscopy to decipher this mechanism.
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معلومات مُعتمدة: R01 GM029595 United States GM NIGMS NIH HHS; R01 GM047274 United States GM NIGMS NIH HHS
المشرفين على المادة: 0 (Protons)
284SYP0193 (Fluorine)
42HK56048U (Tyrosine)
EC 1.17.4.- (Ribonucleotide Reductases)
تواريخ الأحداث: Date Created: 20220602 Date Completed: 20220630 Latest Revision: 20220801
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC9248007
DOI: 10.1021/jacs.2c02906
PMID: 35652913
قاعدة البيانات: MEDLINE
الوصف
تدمد:1520-5126
DOI:10.1021/jacs.2c02906