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Instruments / Technical Area	Publication Details	Published	Actions
I20-Scanning-X-ray spectroscopy (XAS/XES)	Elucidating polyphosphate anion binding to lanthanide complexes using EXAFS and pulsed EPR Spectroscopy Hannah K. Pyle , Martyna Judd , Anthony Barancewicz , Alexander J. Mayer , Nicholas Cox , Simon A. Kondrat , Stephen J. Butler Inorganic Chemistry DOI: 10.1021/acs.inorgchem.4c03399 Diamond Proposal Number(s): [29024] Open Access Show Abstract ▼ Abstract: Reversible anion binding to lanthanide complexes in aqueous solution has emerged as an effective method for anion sensing. Through careful design of the organic ligand, luminescent lanthanide complexes capable of binding biologically relevant anions in a bidentate or monodentate manner can be realized. While single-crystal X-ray diffraction analyses and NMR spectroscopy have revealed the structural geometry of several host–guest complexes, the challenge remains in designing preorganized lanthanide receptors with enhanced anion selectivity for broader applications in diagnostics and bioimaging. To address this challenge, innovative and complementary methods to investigate host-anion binding geometry are becoming increasingly important. Herein, we demonstrate the combined use of Eu L3-edge extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) spectroscopy to elucidate the binding of nucleoside phosphates (ATP, ADP, and AMP) to a cationic lanthanide complex. We establish that ATP unequivocally binds the lanthanide center in a bidentate manner in water, while ADP adopts both bidentate and monodentate modes, and AMP binds in a monodentate manner. This interdisciplinary approach provides deeper insight into lanthanide host–guest chemistry in solution, laying the groundwork for designing emissive probes that undergo specific anion-induced structural changes and elicit desired optical responses upon binding.	Oct 2024
B21-High Throughput SAXS I24-Microfocus Macromolecular Crystallography	Metal-free ribonucleotide reduction powered by a DOPA radical in Mycoplasma pathogens Vivek Srinivas , Hugo Lebrette , Daniel Lundin , Yuri Kutin , Margareta Sahlin , Michael Lerche , Jürgen Eirich , Rui M. M. Branca , Nicholas Cox , Britt-Marie Sjöberg , Martin Högbom Nature 47 DOI: 10.1038/s41586-018-0653-6 Diamond Proposal Number(s): [11265, 15806] Show Abstract ▼ Abstract: Ribonucleotide reductase (RNR) catalyses the only known de novo pathway for the production of all four deoxyribonucleotides that are required for DNA synthesis1,2. It is essential for all organisms that use DNA as their genetic material and is a current drug target3,4. Since the discovery that iron is required for function in the aerobic, class I RNR found in all eukaryotes and many bacteria, a dinuclear metal site has been viewed as necessary to generate and stabilize the catalytic radical that is essential for RNR activity5,6,7. Here we describe a group of RNR proteins in Mollicutes—including Mycoplasma pathogens—that possess a metal-independent stable radical residing on a modified tyrosyl residue. Structural, biochemical and spectroscopic characterization reveal a stable 3,4-dihydroxyphenylalanine (DOPA) radical species that directly supports ribonucleotide reduction in vitro and in vivo. This observation overturns the presumed requirement for a dinuclear metal site in aerobic ribonucleotide reductase. The metal-independent radical requires new mechanisms for radical generation and stabilization, processes that are targeted by RNR inhibitors. It is possible that this RNR variant provides an advantage under metal starvation induced by the immune system. Organisms that encode this type of RNR—some of which are developing resistance to antibiotics—are involved in diseases of the respiratory, urinary and genital tracts. Further characterization of this RNR family and its mechanism of cofactor generation will provide insight into new enzymatic chemistry and be of value in devising strategies to combat the pathogens that utilize it. We propose that this RNR subclass is denoted class Ie.	Oct 2018

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