Tracking the redox reaction of the iron enzyme ribonucleotide reductase using continuous SerialED and SFX

), and re-oxidized states at ∼1.8 Å resolution, capturing three points in a redox reaction. These results demonstrate that c-SerialED can track reversible changes at the redox-site, enabling future time-resolved studies. Comparison between c-SerialED structures and SFX diffraction and emission data confirmed minimal radiation damage. Furthermore, previously reported structures use mercury in the crystallization condition and show mercury-induced conformational changes. Here, we use mercury-free crystallization conditions and reveal a water molecule in the redox center of the reduced state, absent in the previous structures, making these structures more representative of the physiological state.

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Publication Details

Journal
Structure
Published
2026-05-01
DOI
https://doi.org/10.1016/j.str.2026.03.006
Primary Topic
Metal-Catalyzed Oxygenation Mechanisms
Type
article
Field-Weighted Citation Impact
0.00

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article

Tracking the redox reaction of the iron enzyme ribonucleotide reductase using continuous SerialED and SFX

Aaron S. Brewster, Hiroki Makita, Martin Högbom, Oskar Aurelius et al.
Structure
Metal-Catalyzed Oxygenation Mechanisms
article

Tracking the redox reaction of the iron enzyme ribonucleotide reductase using continuous SerialED and SFX

Aaron S. Brewster, Hiroki Makita, Martin Högbom, Oskar Aurelius, Daniel J. Rosenberg, A. Batyuk, Hugo Lebrette, Vittal K. Yachandra, Juliane John, David Moreau, Nicholas K. Sauter, Roberto Alonso‐Mori, Asmit Bhowmick, Daniel W. Paley⧓, Natalie Minnetian, Jan Kern, Buster Blomberg, Xiaodong Zou, Hongyi Xu, Philipp S. Simon, Rahul Bannerjee, Vivek Srinivas, Kuntal Chatterjee, Laura Pacoste, Rohit Kumar, Junko Yano, Leland B. Gee, Gerhard Hofer
article en

Abstract

), and re-oxidized states at ∼1.8 Å resolution, capturing three points in a redox reaction. These results demonstrate that c-SerialED can track reversible changes at the redox-site, enabling future time-resolved studies. Comparison between c-SerialED structures and SFX diffraction and emission data confirmed minimal radiation damage. Furthermore, previously reported structures use mercury in the crystallization condition and show mercury-induced conformational changes. Here, we use mercury-free crystallization conditions and reveal a water molecule in the redox center of the reduced state, absent in the previous structures, making these structures more representative of the physiological state.

Structure
Centre National de la Recherche Scientifique (FR), Lawrence Berkeley National Laboratory (US), Stockholm University (SE), TU Dortmund University (DE), Science for Life Laboratory (SE), SLAC National Accelerator Laboratory (US), MAX IV Laboratory (SE), Linac Coherent Light Source (US), Laboratoire de Microbiologie et Génétique Moléculaires (FR), Auburn University (US)
Foundation for the National Institutes of Health, National Energy Research Scientific Computing Center, Knut och Alice Wallenbergs Stiftelse, Vetenskapsrådet, National Institute of General Medical Sciences, SLAC National Accelerator Laboratory
Openalex Percentile: Top 13%
Metal-Catalyzed Oxygenation Mechanisms
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