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

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Hecker,  F.
Research Group of Electron Paramagnetic Resonance, MPI for Biophysical Chemistry, Max Planck Society;

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Bennati,  M.
Research Group of Electron Paramagnetic Resonance, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

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.


Cite as: http://hdl.handle.net/21.11116/0000-0008-7DA0-7
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.