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  Detection of water molecules on the radical transfer pathway of ribonucleotide reductase by 17O electron–nuclear double resonance spectroscopy

Hecker, F., Stubbe, J., & Bennati, M. (2021). Detection of water molecules on the radical transfer pathway of ribonucleotide reductase by 17O electron–nuclear double resonance spectroscopy. The Journal of the American Chemical Society, In Press. doi:10.1021/jacs.1c01359.

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 Creators:
Hecker, F.1, Author              
Stubbe, J., Author
Bennati, M.1, Author              
Affiliations:
1Research Group of Electron Paramagnetic Resonance, MPI for Biophysical Chemistry, Max Planck Society, ou_578606              

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Free keywords: Peptides and proteins, Proton coupled electron transfer, Molecules, Electron paramagnetic resonance spectroscopy, Quantum mechanics
 Abstract: 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 17O high-frequency electron–nuclear double resonance (ENDOR) in conjunction with H217O-labeled protein buffer to establish the presence of ordered water molecules at three radical intermediates in an active enzyme complex, the α2β2E. coli ribonucleotide reductase. Our data give unambiguous evidence that all three, individually trapped, intermediates are hyperfine coupled to one water molecule with Tyr-O···17O 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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Language(s): eng - English
 Dates: 2021-05-06
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/jacs.1c01359
 Degree: -

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Title: The Journal of the American Chemical Society
Source Genre: Journal
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Pages: - Volume / Issue: - Sequence Number: In Press Start / End Page: - Identifier: -