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National Academy of Sciences, Proceedings of the National Academy of Sciences, 6(105), p. 1844-1848, 2008

DOI: 10.1073/pnas.0711659105

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Quantum model of catalysis based on a mobile proton revealed by subatomic x-ray and neutron diffraction studies of h-aldose reductase

Journal article published in 2008 by Matthew P. Blakeley, Federico Ruiz ORCID, Raul Cachau, Isabelle Hazemann, Flora Meilleur ORCID, Andre Mitschler, Stephan Ginell, Pavel Afonine, Oscar N. Ventura, Alexandra Cousido-Siah, Michael Haertlein, Andrzej Joachimiak, Dean Myles, Alberto Podjarny
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

We present results of combined studies of the enzyme human aldose reductase (h-AR, 36 kDa) using single-crystal x-ray data (0.66 Å, 100K; 0.80 Å, 15K; 1.75 Å, 293K), neutron Laue data (2.2 Å, 293K), and quantum mechanical modeling. These complementary techniques unveil the internal organization and mobility of the hydrogen bond network that defines the properties of the catalytic engine, explaining how this promiscuous enzyme overcomes the simultaneous requirements of efficiency and promiscuity offering a general mechanistic view for this class of enzymes.