A joint X-ray/neutron diffraction study has enabled the direct observation of a hydronium ion coordinated by three amino-acid residues of an enzyme. This sighting will affect our views on how enzymes transport and use protons.
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References
Kovalevsky, A. Y. et al. Angew. Chem. Int. Ed. http://dx.doi.org/10.1002/anie.201101753 (2011).
Blakeley, M. P., Langan, P., Niimura, N. & Podjarny, A. Curr. Opin. Struct. Biol. 18, 593–600 (2008).
Buhl, M. & Wipff, G. J. Am. Chem. Soc. 124, 4473–4480 (2002).
Boyer, P. D. Trends Biochem. Sci. 13, 5–7 (1988).
Morii, M. et al. J. Biol. Chem. 283, 16876–16884 (2008).
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Davidson, V. The many faces of a proton. Nature Chem 3, 662–663 (2011). https://doi.org/10.1038/nchem.1122
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DOI: https://doi.org/10.1038/nchem.1122
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