دورية أكاديمية
أعرض في EDS

Detection of Water Molecules on the Radical Transfer Pathway of Ribonucleotide Reductase by 17 O Electron-Nuclear Double Resonance Spectroscopy.

التفاصيل البيبلوغرافية
العنوان: Detection of Water Molecules on the Radical Transfer Pathway of Ribonucleotide Reductase by 17 O Electron-Nuclear Double Resonance Spectroscopy.
المؤلفون: Hecker F; Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany., Stubbe J; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 20139, United States., Bennati M; Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.; Department of Chemistry, Georg-August-University, 37077 Göttingen, Germany.
المصدر: Journal of the American Chemical Society [J Am Chem Soc] 2021 May 19; Vol. 143 (19), pp. 7237-7241. Date of Electronic Publication: 2021 May 06.
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: Ribonucleotide Reductases/*metabolism , Tyrosine/*metabolism , Water/*analysis, Density Functional Theory ; Electron Spin Resonance Spectroscopy ; Electron Transport ; Electrons ; Escherichia coli/enzymology ; Free Radicals/chemistry ; Free Radicals/metabolism ; Oxygen Isotopes ; Ribonucleotide Reductases/chemistry ; Tyrosine/chemistry
مستخلص: The role of water in biological proton-coupled electron transfer (PCET) is emerging as a key for understanding mechanistic details at atomic resolution. Here we demonstrate 17 O high-frequency electron-nuclear double resonance (ENDOR) in conjunction with H 2 17 O-labeled protein buffer to establish the presence of ordered water molecules at three radical intermediates in an active enzyme complex, the α 2 β 2 E. coli ribonucleotide reductase. Our data give unambiguous evidence that all three, individually trapped, intermediates are hyperfine coupled to one water molecule with Tyr-O··· 17 O distances in the range 2.8-3.1 Å. The availability of this structural information will allow for quantitative models of PCET in this prototype enzyme. The results also provide a spectroscopic signature for water H-bonded to a tyrosyl radical.
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المشرفين على المادة: 0 (Free Radicals)
0 (Oxygen Isotopes)
0 (Oxygen-17)
059QF0KO0R (Water)
42HK56048U (Tyrosine)
EC 1.17.4.- (Ribonucleotide Reductases)
تواريخ الأحداث: Date Created: 20210506 Date Completed: 20211229 Latest Revision: 20240402
رمز التحديث: 20240402
مُعرف محوري في PubMed: PMC8154519
DOI: 10.1021/jacs.1c01359
PMID: 33957040
قاعدة البيانات: MEDLINE
الوصف
تدمد:1520-5126
DOI:10.1021/jacs.1c01359